3oyf - Revision history

OCA at 09:46, 6 September 2023

2023-09-06T09:46:05Z

←Older revision		Revision as of 09:46, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3oyf' size='340' side='right'caption='[[3oyf]], [[Resolution\|resolution]] 2.51Å' scene=''>		<StructureSection load='3oyf' size='340' side='right'caption='[[3oyf]], [[Resolution\|resolution]] 2.51Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oyf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Foamv Foamv~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OYF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oyf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OYF FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZYP:5-(1,1-DIOXIDO-1,2-THIAZINAN-2-YL)-N-(4-FLUOROBENZYL)-8-HYDROXY-1,6-NAPHTHYRIDINE-7-CARBOXAMIDE'>ZYP</scene>~~</td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.51Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dlr\|3dlr]], [[3l2q\|3l2q]], [[3l2r\|3l2r]], [[3l2u\|3l2u]], [[3l2v\|3l2v]], [[3l2w\|3l2w]], [[3oy9\|3oy9]], [[3oya\|3oya]], [[3oyb\|3oyb]], [[3oyc\|3oyc]], [[3oyd\|3oyd]], [[3oye\|3oye]], [[3oyg\|3oyg]], [[3oyh\|3oyh]], [[3oyi\|3oyi]], [[3oyj\|3oyj]], [[3oyk\|3oyk]], [[3oyl\|3oyl]], [[3oym\|3oym]], [[3oyn\|3oyn]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZYP:5-(1,1-DIOXIDO-1,2-THIAZINAN-2-YL)-N-(4-FLUOROBENZYL)-8-HYDROXY-1,6-NAPHTHYRIDINE-7-CARBOXAMIDE'>ZYP</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11963 FOAMV])~~</td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyf OCA], [https://pdbe.org/3oyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oyf RCSB], [https://www.ebi.ac.uk/pdbsum/3oyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oyf ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyf OCA], [https://pdbe.org/3oyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oyf RCSB], [https://www.ebi.ac.uk/pdbsum/3oyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oyf ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/POL_FOAMV POL_FOAMV]] The aspartyl protease activity mediates proteolytic cleavages of Gag and Pol polyproteins. The reverse transcriptase (RT) activity converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell (early reverse transcription) or after proviral DNA transcription (late reverse transcription). RT consists of a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA-Lys1,2 binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising at least the viral genome, matrix protein, and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from the 3' end of the viral DNA right (U5) end, leaving the left (U3) intact. In the second step, the PIC enters cell nucleus. This process is mediated through the integrase and allows the virus to infect both dividing (nuclear membrane disassembled) and G1/S-arrested cells (active translocation), but with no viral gene expression in the latter. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. It is however not clear how integration then proceeds to resolve the asymmetrical cleavage of viral DNA (By similarity).	+	[https://www.uniprot.org/uniprot/POL_FOAMV POL_FOAMV] The aspartyl protease activity mediates proteolytic cleavages of Gag and Pol polyproteins. The reverse transcriptase (RT) activity converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell (early reverse transcription) or after proviral DNA transcription (late reverse transcription). RT consists of a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA-Lys1,2 binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising at least the viral genome, matrix protein, and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from the 3' end of the viral DNA right (U5) end, leaving the left (U3) intact. In the second step, the PIC enters cell nucleus. This process is mediated through the integrase and allows the virus to infect both dividing (nuclear membrane disassembled) and G1/S-arrested cells (active translocation), but with no viral gene expression in the latter. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. It is however not clear how integration then proceeds to resolve the asymmetrical cleavage of viral DNA (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Foamv~~]]	+	[[Category: Human spumaretrovirus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cherepanov, P]]	+	[[Category: Cherepanov P]]
-	[[Category: Hare, S]]	+	[[Category: Hare S]]
-	~~[[Category: Dna integration]]~~	+
-	~~[[Category: Dna-binding]]~~	+
-	~~[[Category: Dna-binding protein-dna complex]]~~	+
-	~~[[Category: Endonuclease]]~~	+
-	~~[[Category: Hhcc motif]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Multifunctional enzyme]]~~	+
-	~~[[Category: Nuclease]]~~	+
-	~~[[Category: Nucleotidyltransferase]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Protein-dna complex]]~~	+
-	~~[[Category: Recombination]]~~	+
-	~~[[Category: Tetramer]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Viral nucleoprotein]]~~	+
-	~~[[Category: Viral protein]]~~	+
-	~~[[Category: Viral protein-dna complex]]~~	+
-	~~[[Category: Virion]]~~	+
-	~~[[Category: Zinc binding~~]]	+

OCA at 11:03, 18 May 2022

2022-05-18T11:03:16Z

←Older revision		Revision as of 11:03, 18 May 2022
Line 1:		Line 1:

	==Crystal structure of the Prototype Foamy Virus (PFV) intasome in complex with magnesium and the INSTI L-870,810==		==Crystal structure of the Prototype Foamy Virus (PFV) intasome in complex with magnesium and the INSTI L-870,810==
-	<StructureSection load='3oyf' size='340' side='right' caption='[[3oyf]], [[Resolution\|resolution]] 2.51Å' scene=''>	+	<StructureSection load='3oyf' size='340' side='right'caption='[[3oyf]], [[Resolution\|resolution]] 2.51Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oyf]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Foamv Foamv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3OYF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oyf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Foamv Foamv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OYF FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZYP:5-(1,1-DIOXIDO-1,2-THIAZINAN-2-YL)-N-(4-FLUOROBENZYL)-8-HYDROXY-1,6-NAPHTHYRIDINE-7-CARBOXAMIDE'>ZYP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZYP:5-(1,1-DIOXIDO-1,2-THIAZINAN-2-YL)-N-(4-FLUOROBENZYL)-8-HYDROXY-1,6-NAPHTHYRIDINE-7-CARBOXAMIDE'>ZYP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3dlr\|3dlr]], [[3l2q\|3l2q]], [[3l2r\|3l2r]], [[3l2u\|3l2u]], [[3l2v\|3l2v]], [[3l2w\|3l2w]], [[3oy9\|3oy9]], [[3oya\|3oya]], [[3oyb\|3oyb]], [[3oyc\|3oyc]], [[3oyd\|3oyd]], [[3oye\|3oye]], [[3oyg\|3oyg]], [[3oyh\|3oyh]], [[3oyi\|3oyi]], [[3oyj\|3oyj]], [[3oyk\|3oyk]], [[3oyl\|3oyl]], [[3oym\|3oym]], [[3oyn\|3oyn]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dlr\|3dlr]], [[3l2q\|3l2q]], [[3l2r\|3l2r]], [[3l2u\|3l2u]], [[3l2v\|3l2v]], [[3l2w\|3l2w]], [[3oy9\|3oy9]], [[3oya\|3oya]], [[3oyb\|3oyb]], [[3oyc\|3oyc]], [[3oyd\|3oyd]], [[3oye\|3oye]], [[3oyg\|3oyg]], [[3oyh\|3oyh]], [[3oyi\|3oyi]], [[3oyj\|3oyj]], [[3oyk\|3oyk]], [[3oyl\|3oyl]], [[3oym\|3oym]], [[3oyn\|3oyn]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POL ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11963 FOAMV])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11963 FOAMV])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3oyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyf OCA], [~~http~~://pdbe.org/3oyf PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3oyf RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3oyf PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3oyf ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyf OCA], [https://pdbe.org/3oyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oyf RCSB], [https://www.ebi.ac.uk/pdbsum/3oyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oyf ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/POL_FOAMV POL_FOAMV]] The aspartyl protease activity mediates proteolytic cleavages of Gag and Pol polyproteins. The reverse transcriptase (RT) activity converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell (early reverse transcription) or after proviral DNA transcription (late reverse transcription). RT consists of a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA-Lys1,2 binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising at least the viral genome, matrix protein, and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from the 3' end of the viral DNA right (U5) end, leaving the left (U3) intact. In the second step, the PIC enters cell nucleus. This process is mediated through the integrase and allows the virus to infect both dividing (nuclear membrane disassembled) and G1/S-arrested cells (active translocation), but with no viral gene expression in the latter. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. It is however not clear how integration then proceeds to resolve the asymmetrical cleavage of viral DNA (By similarity).	+	[[https://www.uniprot.org/uniprot/POL_FOAMV POL_FOAMV]] The aspartyl protease activity mediates proteolytic cleavages of Gag and Pol polyproteins. The reverse transcriptase (RT) activity converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell (early reverse transcription) or after proviral DNA transcription (late reverse transcription). RT consists of a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA-Lys1,2 binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising at least the viral genome, matrix protein, and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from the 3' end of the viral DNA right (U5) end, leaving the left (U3) intact. In the second step, the PIC enters cell nucleus. This process is mediated through the integrase and allows the virus to infect both dividing (nuclear membrane disassembled) and G1/S-arrested cells (active translocation), but with no viral gene expression in the latter. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. It is however not clear how integration then proceeds to resolve the asymmetrical cleavage of viral DNA (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[Retroviral ~~Integrase~~\|Retroviral ~~Integrase~~]]	+	*[[Retroviral integrase 3D structures\|Retroviral integrase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Foamv]]		[[Category: Foamv]]
		+	[[Category: Large Structures]]
	[[Category: Cherepanov, P]]		[[Category: Cherepanov, P]]
	[[Category: Hare, S]]		[[Category: Hare, S]]

OCA at 11:19, 4 August 2016

2016-08-04T11:19:26Z

←Older revision		Revision as of 11:19, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the Prototype Foamy Virus (PFV) intasome in complex with magnesium and the INSTI L-870,810==		==Crystal structure of the Prototype Foamy Virus (PFV) intasome in complex with magnesium and the INSTI L-870,810==
	<StructureSection load='3oyf' size='340' side='right' caption='[[3oyf]], [[Resolution\|resolution]] 2.51Å' scene=''>		<StructureSection load='3oyf' size='340' side='right' caption='[[3oyf]], [[Resolution\|resolution]] 2.51Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oyf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Human_spumaretrovirus Human spumaretrovirus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OYF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oyf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Foamv Foamv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OYF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZYP:5-(1,1-DIOXIDO-1,2-THIAZINAN-2-YL)-N-(4-FLUOROBENZYL)-8-HYDROXY-1,6-NAPHTHYRIDINE-7-CARBOXAMIDE'>ZYP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZYP:5-(1,1-DIOXIDO-1,2-THIAZINAN-2-YL)-N-(4-FLUOROBENZYL)-8-HYDROXY-1,6-NAPHTHYRIDINE-7-CARBOXAMIDE'>ZYP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3dlr\|3dlr]], [[3l2q\|3l2q]], [[3l2r\|3l2r]], [[3l2u\|3l2u]], [[3l2v\|3l2v]], [[3l2w\|3l2w]], [[3oy9\|3oy9]], [[3oya\|3oya]], [[3oyb\|3oyb]], [[3oyc\|3oyc]], [[3oyd\|3oyd]], [[3oye\|3oye]], [[3oyg\|3oyg]], [[3oyh\|3oyh]], [[3oyi\|3oyi]], [[3oyj\|3oyj]], [[3oyk\|3oyk]], [[3oyl\|3oyl]], [[3oym\|3oym]], [[3oyn\|3oyn]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3dlr\|3dlr]], [[3l2q\|3l2q]], [[3l2r\|3l2r]], [[3l2u\|3l2u]], [[3l2v\|3l2v]], [[3l2w\|3l2w]], [[3oy9\|3oy9]], [[3oya\|3oya]], [[3oyb\|3oyb]], [[3oyc\|3oyc]], [[3oyd\|3oyd]], [[3oye\|3oye]], [[3oyg\|3oyg]], [[3oyh\|3oyh]], [[3oyi\|3oyi]], [[3oyj\|3oyj]], [[3oyk\|3oyk]], [[3oyl\|3oyl]], [[3oym\|3oym]], [[3oyn\|3oyn]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11963 ~~Human spumaretrovirus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11963 FOAMV])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oyf RCSB], [http://www.ebi.ac.uk/pdbsum/3oyf PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyf OCA], [http://pdbe.org/3oyf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oyf RCSB], [http://www.ebi.ac.uk/pdbsum/3oyf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oyf ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3oyf" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human spumaretrovirus~~]]	+	[[Category: Foamv]]
	[[Category: Cherepanov, P]]		[[Category: Cherepanov, P]]
	[[Category: Hare, S]]		[[Category: Hare, S]]

OCA at 13:48, 24 December 2014

2014-12-24T13:48:06Z

←Older revision		Revision as of 13:48, 24 December 2014
Line 8:		Line 8:
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oyf RCSB], [http://www.ebi.ac.uk/pdbsum/3oyf PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oyf RCSB], [http://www.ebi.ac.uk/pdbsum/3oyf PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POL_FOAMV POL_FOAMV]] The aspartyl protease activity mediates proteolytic cleavages of Gag and Pol polyproteins. The reverse transcriptase (RT) activity converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell (early reverse transcription) or after proviral DNA transcription (late reverse transcription). RT consists of a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA-Lys1,2 binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising at least the viral genome, matrix protein, and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from the 3' end of the viral DNA right (U5) end, leaving the left (U3) intact. In the second step, the PIC enters cell nucleus. This process is mediated through the integrase and allows the virus to infect both dividing (nuclear membrane disassembled) and G1/S-arrested cells (active translocation), but with no viral gene expression in the latter. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. It is however not clear how integration then proceeds to resolve the asymmetrical cleavage of viral DNA (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 12:58, 9 December 2014

2014-12-09T12:58:46Z

←Older revision		Revision as of 12:58, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3oyf.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of the Prototype Foamy Virus (PFV) intasome in complex with magnesium and the INSTI L-870,810==
		+	<StructureSection load='3oyf' size='340' side='right' caption='[[3oyf]], [[Resolution\|resolution]] 2.51Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3oyf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OYF FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZYP:5-(1,1-DIOXIDO-1,2-THIAZINAN-2-YL)-N-(4-FLUOROBENZYL)-8-HYDROXY-1,6-NAPHTHYRIDINE-7-CARBOXAMIDE'>ZYP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3dlr\|3dlr]], [[3l2q\|3l2q]], [[3l2r\|3l2r]], [[3l2u\|3l2u]], [[3l2v\|3l2v]], [[3l2w\|3l2w]], [[3oy9\|3oy9]], [[3oya\|3oya]], [[3oyb\|3oyb]], [[3oyc\|3oyc]], [[3oyd\|3oyd]], [[3oye\|3oye]], [[3oyg\|3oyg]], [[3oyh\|3oyh]], [[3oyi\|3oyi]], [[3oyj\|3oyj]], [[3oyk\|3oyk]], [[3oyl\|3oyl]], [[3oym\|3oym]], [[3oyn\|3oyn]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11963 Human spumaretrovirus])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oyf RCSB], [http://www.ebi.ac.uk/pdbsum/3oyf PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The development of HIV integrase (IN) strand transfer inhibitors (INSTIs) and our understanding of viral resistance to these molecules have been hampered by a paucity of available structural data. We recently reported cocrystal structures of the prototype foamy virus (PFV) intasome with raltegravir and elvitegravir, establishing the general INSTI binding mode. We now present an expanded set of cocrystal structures containing PFV intasomes complexed with first- and second-generation INSTIs at resolutions of up to 2.5 A. Importantly, the improved resolution allowed us to refine the complete coordination spheres of the catalytic metal cations within the INSTI-bound intasome active site. We show that like the Q148H/G140S and N155H HIV-1 IN variants, the analogous S217H and N224H PFV INs display reduced sensitivity to raltegravir in vitro. Crystal structures of the mutant PFV intasomes in INSTI-free and -bound forms revealed that the amino acid substitutions necessitate considerable conformational rearrangements within the IN active site to accommodate an INSTI, thus explaining their adverse effects on raltegravir antiviral activity. Furthermore, our structures predict physical proximity and an interaction between HIV-1 IN mutant residues His148 and Ser/Ala140, rationalizing the coevolution of Q148H and G140S/A mutations in drug-resistant viral strains.

-	~~{{STRUCTURE_3oyf\| PDB=3oyf \| SCENE= }}~~	+	Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance.,Hare S, Vos AM, Clayton RF, Thuring JW, Cummings MD, Cherepanov P Proc Natl Acad Sci U S A. 2010 Oct 28. PMID:21030679<ref>PMID:21030679</ref>

-	~~===Crystal structure~~ of the ~~Prototype Foamy Virus (PFV) intasome in complex with magnesium and the INSTI L-870,810===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_21030679}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3oyf]] is a 4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Human_spumaretrovirus Human spumaretrovirus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA].~~	+

	==See Also==		==See Also==
	*[[Retroviral Integrase\|Retroviral Integrase]]		*[[Retroviral Integrase\|Retroviral Integrase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:021030679<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Human spumaretrovirus]]		[[Category: Human spumaretrovirus]]
-	[[Category: Cherepanov, P.]]	+	[[Category: Cherepanov, P]]
-	[[Category: Hare, S.]]	+	[[Category: Hare, S]]
	[[Category: Dna integration]]		[[Category: Dna integration]]
	[[Category: Dna-binding]]		[[Category: Dna-binding]]

OCA at 06:09, 20 October 2012

2012-10-20T06:09:34Z

←Older revision		Revision as of 06:09, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3oyf]] is a 4 chain structure ~~of [[Retroviral Integrase]]~~ with sequence from [http://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA].	+	[[3oyf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA].

	==See Also==		==See Also==

OCA at 12:18, 25 July 2012

2012-07-25T12:18:17Z

←Older revision		Revision as of 12:18, 25 July 2012
Line 1:		Line 1:
	[[Image:3oyf.png\|left\|200px]]		[[Image:3oyf.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_3oyf\| PDB=3oyf \| SCENE= }}		{{STRUCTURE_3oyf\| PDB=3oyf \| SCENE= }}

	===Crystal structure of the Prototype Foamy Virus (PFV) intasome in complex with magnesium and the INSTI L-870,810===		===Crystal structure of the Prototype Foamy Virus (PFV) intasome in complex with magnesium and the INSTI L-870,810===

-
-	<!--
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	{{ABSTRACT_PUBMED_21030679}}		{{ABSTRACT_PUBMED_21030679}}

	==About this Structure==		==About this Structure==
-	[[3oyf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA].	+	[[3oyf]] is a 4 chain structure of [[Retroviral Integrase]] with sequence from [http://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA].
		+
		+	==See Also==
		+	*[[Retroviral Integrase\|Retroviral Integrase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~21030679~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021030679</ref><references group="xtra"/>
	[[Category: Human spumaretrovirus]]		[[Category: Human spumaretrovirus]]
	[[Category: Cherepanov, P.]]		[[Category: Cherepanov, P.]]
	[[Category: Hare, S.]]		[[Category: Hare, S.]]
		+	[[Category: Dna integration]]
		+	[[Category: Dna-binding]]
		+	[[Category: Dna-binding protein-dna complex]]
		+	[[Category: Endonuclease]]
		+	[[Category: Hhcc motif]]
		+	[[Category: Inhibitor]]
		+	[[Category: Metal-binding]]
		+	[[Category: Multifunctional enzyme]]
		+	[[Category: Nuclease]]
		+	[[Category: Nucleotidyltransferase]]
		+	[[Category: Nucleus]]
		+	[[Category: Protein-dna complex]]
		+	[[Category: Recombination]]
		+	[[Category: Tetramer]]
		+	[[Category: Transferase]]
		+	[[Category: Viral nucleoprotein]]
		+	[[Category: Viral protein]]
		+	[[Category: Viral protein-dna complex]]
		+	[[Category: Virion]]
		+	[[Category: Zinc binding]]

OCA: Protected "3oyf" [edit=sysop:move=sysop]

2011-03-30T07:27:04Z

Protected "3oyf" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:27, 30 March 2011

OCA at 07:27, 30 March 2011

2011-03-30T07:27:02Z

←Older revision		Revision as of 07:27, 30 March 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3oyf.png\|left\|200px]]		[[Image:3oyf.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~3OYF~~ is a 4 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA].	+	[[3oyf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYF OCA].

	==Reference==		==Reference==
Line 27:		Line 26:
	[[Category: Cherepanov, P.]]		[[Category: Cherepanov, P.]]
	[[Category: Hare, S.]]		[[Category: Hare, S.]]
-	[[Category: Dna integration]]
-	[[Category: Dna-binding]]
-	[[Category: Dna-binding protein-dna complex]]
-	[[Category: Endonuclease]]
-	[[Category: Hhcc motif]]
-	[[Category: Inhibitor]]
-	[[Category: Metal-binding]]
-	[[Category: Multifunctional enzyme]]
-	[[Category: Nuclease]]
-	[[Category: Nucleotidyltransferase]]
-	[[Category: Nucleus]]
-	[[Category: Protein-dna complex]]
-	[[Category: Recombination]]
-	[[Category: Tetramer]]
-	[[Category: Transferase]]
-	[[Category: Viral nucleoprotein]]
-	[[Category: Viral protein]]
-	[[Category: Viral protein-dna complex]]
-	[[Category: Virion]]
-	[[Category: Zinc binding]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 1 10:57:32 2010''

OCA at 07:45, 1 December 2010

2010-12-01T07:45:45Z

←Older revision		Revision as of 07:45, 1 December 2010
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:3oyf.~~jpg~~\|left\|200px]]	+	[[Image:3oyf.png\|left\|200px]]

	<!--		<!--
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	[[Category: Zinc binding]]		[[Category: Zinc binding]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Nov 18 00~~:54:38 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 1 10:57:32 2010''