4dm0 - Revision history

OCA at 14:38, 14 March 2024

OCA — Thu, 14 Mar 2024 14:38:52 GMT

←Older revision		Revision as of 14:38, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dm0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mur 1mur] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DM0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dm0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mur 1mur] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DM0 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=4dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm0 OCA], [https://pdbe.org/4dm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dm0 RCSB], [https://www.ebi.ac.uk/pdbsum/4dm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm0 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=4dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm0 OCA], [https://pdbe.org/4dm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dm0 RCSB], [https://www.ebi.ac.uk/pdbsum/4dm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX]] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref> <ref>PMID:6291786</ref> <ref>PMID:6303899</ref> <ref>PMID:1310499</ref> <ref>PMID:8226636</ref> <ref>PMID:8871560</ref> <ref>PMID:11877443</ref> <ref>PMID:12367522</ref>	+	[https://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref> <ref>PMID:6291786</ref> <ref>PMID:6303899</ref> <ref>PMID:1310499</ref> <ref>PMID:8226636</ref> <ref>PMID:8871560</ref> <ref>PMID:11877443</ref> <ref>PMID:12367522</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	A synaptic complex of Tn5 transposase with an extended outside end DNA duplex was prepared and crystallized, and its crystal structure was determined in an effort to reveal the role of metal ions in catalysis. Two Mn2+ ions bound to the active site when a single nucleotide of donor DNA was added to the 3' end of the transferred strand. Marked conformational changes were observed in the DNA bases closest to the active site. The position of the metal ions and the conformational changes of the DNA provide insight into the mechanism of hairpin formation and cleavage, and is consistent with a two-metal model for catalysis.	+
-		+
-	~~Two-metal active site binding of a Tn5 transposase synaptic complex.,Lovell S, Goryshin IY, Reznikoff WR, Rayment I Nat Struct Biol. 2002 Apr;9(4):278-81. PMID:11896402<ref>PMID:11896402</ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4dm0" style="background-color:#fffaf0;"></div~~>	+

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

OCA at 08:27, 21 September 2022

OCA — Wed, 21 Sep 2022 08:27:34 GMT

←Older revision		Revision as of 08:27, 21 September 2022
Line 1:		Line 1:

	==TN5 transposase: 20MER OUTSIDE END 2 MN complex==		==TN5 transposase: 20MER OUTSIDE END 2 MN complex==
-	<StructureSection load='4dm0' size='340' side='right' caption='[[4dm0]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='4dm0' size='340' side='right'caption='[[4dm0]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dm0]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mur 1mur] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4DM0 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dm0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mur 1mur] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DM0 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1muh\|1muh]], [[1mus\|1mus]]</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=4dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm0 OCA], [https://pdbe.org/4dm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dm0 RCSB], [https://www.ebi.ac.uk/pdbsum/4dm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm0 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tnpA, tnp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm0 OCA], [~~http~~://pdbe.org/4dm0 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4dm0 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4dm0 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm0 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX]] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref> <ref>PMID:6291786</ref> <ref>PMID:6303899</ref> <ref>PMID:1310499</ref> <ref>PMID:8226636</ref> <ref>PMID:8871560</ref> <ref>PMID:11877443</ref> <ref>PMID:12367522</ref>	+	[[https://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX]] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref> <ref>PMID:6291786</ref> <ref>PMID:6303899</ref> <ref>PMID:1310499</ref> <ref>PMID:8226636</ref> <ref>PMID:8871560</ref> <ref>PMID:11877443</ref> <ref>PMID:12367522</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4dm0" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4dm0" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Transposase 3D structures\|Transposase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
-	[[Category: Goryshin~~, I Y~~]]	+	[[Category: Large Structures]]
-	[[Category: Klenchin~~, V A~~]]	+	[[Category: Goryshin IY]]
-	[[Category: Lovell, S]]	+	[[Category: Klenchin VA]]
-	[[Category: Rayment, I]]	+	[[Category: Lovell S]]
-	[[Category: Reznikoff~~, W R]]~~	+	[[Category: Rayment I]]
-	~~[[Category: Dna recombination-dna complex]]~~	+	[[Category: Reznikoff WR]]
-	~~[[Category: Hydrolase-dna complex]]~~	+
-	~~[[Category: Protein-dna complex]]~~	+
-	~~[[Category: Ribonuclease h-like motif]]~~	+
-	~~[[Category: Synaptic complex]]~~	+
-	~~[[Category: Transposase~~]]	+

OCA at 07:54, 15 November 2017

OCA — Wed, 15 Nov 2017 07:54:19 GMT

←Older revision		Revision as of 07:54, 15 November 2017
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4dm0" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4dm0" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Transposase\|Transposase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 05:00, 5 August 2016

OCA — Fri, 05 Aug 2016 05:00:27 GMT

←Older revision		Revision as of 05:00, 5 August 2016
Line 1:		Line 1:
		+
	==TN5 transposase: 20MER OUTSIDE END 2 MN complex==		==TN5 transposase: 20MER OUTSIDE END 2 MN complex==
	<StructureSection load='4dm0' size='340' side='right' caption='[[4dm0]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4dm0' size='340' side='right' caption='[[4dm0]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dm0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia~~ coli]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DM0 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dm0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mur 1mur] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DM0 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1muh\|1muh]], [[1mus\|1mus]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1muh\|1muh]], [[1mus\|1mus]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tnpA, tnp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 ~~Escherichia~~ coli])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tnpA, tnp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dm0 RCSB], [http://www.ebi.ac.uk/pdbsum/4dm0 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=4dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm0 OCA], [http://pdbe.org/4dm0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dm0 RCSB], [http://www.ebi.ac.uk/pdbsum/4dm0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm0 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 4dm0" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia~~ coli]]	+	[[Category: Bacillus coli migula 1895]]
	[[Category: Goryshin, I Y]]		[[Category: Goryshin, I Y]]
	[[Category: Klenchin, V A]]		[[Category: Klenchin, V A]]

OCA at 15:58, 25 December 2014

OCA — Thu, 25 Dec 2014 15:58:31 GMT

←Older revision		Revision as of 15:58, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4dm0\| PDB~~=4dm0 \| ~~SCENE~~= }}	+	==TN5 transposase: 20MER OUTSIDE END 2 MN complex==
-	===~~TN5 transposase~~: ~~20MER OUTSIDE END~~ 2 MN ~~complex~~===	+	<StructureSection load='4dm0' size='340' side='right' caption='[[4dm0]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_11896402}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4dm0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DM0 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1muh\|1muh]], [[1mus\|1mus]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tnpA, tnp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=4dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dm0 RCSB], [http://www.ebi.ac.uk/pdbsum/4dm0 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX]] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref> <ref>PMID:6291786</ref> <ref>PMID:6303899</ref> <ref>PMID:1310499</ref> <ref>PMID:8226636</ref> <ref>PMID:8871560</ref> <ref>PMID:11877443</ref> <ref>PMID:12367522</ref>		[[http://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX]] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref> <ref>PMID:6291786</ref> <ref>PMID:6303899</ref> <ref>PMID:1310499</ref> <ref>PMID:8226636</ref> <ref>PMID:8871560</ref> <ref>PMID:11877443</ref> <ref>PMID:12367522</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A synaptic complex of Tn5 transposase with an extended outside end DNA duplex was prepared and crystallized, and its crystal structure was determined in an effort to reveal the role of metal ions in catalysis. Two Mn2+ ions bound to the active site when a single nucleotide of donor DNA was added to the 3' end of the transferred strand. Marked conformational changes were observed in the DNA bases closest to the active site. The position of the metal ions and the conformational changes of the DNA provide insight into the mechanism of hairpin formation and cleavage, and is consistent with a two-metal model for catalysis.
		+
		+	Two-metal active site binding of a Tn5 transposase synaptic complex.,Lovell S, Goryshin IY, Reznikoff WR, Rayment I Nat Struct Biol. 2002 Apr;9(4):278-81. PMID:11896402<ref>PMID:11896402</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4dm0]] is~~ a ~~3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes~~ the ~~now removed PDB entries and [http://oca~~.~~weizmann~~.ac.il/~~oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:011896402</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Transposase\|Transposase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Goryshin, I Y.]]	+	[[Category: Goryshin, I Y]]
-	[[Category: Klenchin, V A.]]	+	[[Category: Klenchin, V A]]
-	[[Category: Lovell, S.]]	+	[[Category: Lovell, S]]
-	[[Category: Rayment, I.]]	+	[[Category: Rayment, I]]
-	[[Category: Reznikoff, W R.]]	+	[[Category: Reznikoff, W R]]
	[[Category: Dna recombination-dna complex]]		[[Category: Dna recombination-dna complex]]
	[[Category: Hydrolase-dna complex]]		[[Category: Hydrolase-dna complex]]

OCA at 01:29, 4 April 2013

OCA — Thu, 04 Apr 2013 01:29:41 GMT

←Older revision		Revision as of 01:29, 4 April 2013
Line 4:		Line 4:

	==Function==		==Function==
-	[[http://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX]] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref><ref>PMID:6291786</ref><ref>PMID:6303899</ref><ref>PMID:1310499</ref><ref>PMID:8226636</ref><ref>PMID:8871560</ref><ref>PMID:11877443</ref><ref>PMID:12367522</ref>	+	[[http://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX]] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref> <ref>PMID:6291786</ref> <ref>PMID:6303899</ref> <ref>PMID:1310499</ref> <ref>PMID:8226636</ref> <ref>PMID:8871560</ref> <ref>PMID:11877443</ref> <ref>PMID:12367522</ref>

	==About this Structure==		==About this Structure==

OCA at 08:47, 27 March 2013

OCA — Wed, 27 Mar 2013 08:47:45 GMT

←Older revision		Revision as of 08:47, 27 March 2013
Line 2:		Line 2:
	===TN5 transposase: 20MER OUTSIDE END 2 MN complex===		===TN5 transposase: 20MER OUTSIDE END 2 MN complex===
	{{ABSTRACT_PUBMED_11896402}}		{{ABSTRACT_PUBMED_11896402}}
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX]] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref><ref>PMID:6291786</ref><ref>PMID:6303899</ref><ref>PMID:1310499</ref><ref>PMID:8226636</ref><ref>PMID:8871560</ref><ref>PMID:11877443</ref><ref>PMID:12367522</ref>

	==About this Structure==		==About this Structure==
Line 7:		Line 10:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:011896402</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011896402</ref><references group="xtra"/><references/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Goryshin, I Y.]]		[[Category: Goryshin, I Y.]]

OCA at 10:20, 13 March 2013

OCA — Wed, 13 Mar 2013 10:20:49 GMT

←Older revision		Revision as of 10:20, 13 March 2013
Line 1:		Line 1:
-	[[Image:4dm0.png\|left\|200px]]
-
	{{STRUCTURE_4dm0\| PDB=4dm0 \| SCENE= }}		{{STRUCTURE_4dm0\| PDB=4dm0 \| SCENE= }}
-
	===TN5 transposase: 20MER OUTSIDE END 2 MN complex===		===TN5 transposase: 20MER OUTSIDE END 2 MN complex===
-
	{{ABSTRACT_PUBMED_11896402}}		{{ABSTRACT_PUBMED_11896402}}

OCA at 09:29, 21 November 2012

OCA — Wed, 21 Nov 2012 09:29:33 GMT

←Older revision		Revision as of 09:29, 21 November 2012
Line 5:		Line 5:
	===TN5 transposase: 20MER OUTSIDE END 2 MN complex===		===TN5 transposase: 20MER OUTSIDE END 2 MN complex===

		+	{{ABSTRACT_PUBMED_11896402}}

	==About this Structure==		==About this Structure==

OCA at 13:45, 8 November 2012

OCA — Thu, 08 Nov 2012 13:45:03 GMT

←Older revision		Revision as of 13:45, 8 November 2012
Line 5:		Line 5:
	===TN5 transposase: 20MER OUTSIDE END 2 MN complex===		===TN5 transposase: 20MER OUTSIDE END 2 MN complex===

-	{{ABSTRACT_PUBMED_11896402}}

	==About this Structure==		==About this Structure==