4kgk - Revision history

OCA at 12:12, 1 March 2024

OCA — Fri, 01 Mar 2024 12:12:49 GMT

←Older revision		Revision as of 12:12, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4kgk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis_ATCC_35646 Bacillus thuringiensis serovar israelensis ATCC 35646]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KGK FirstGlance]. <br>		<table><tr><td colspan='2'>[[4kgk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis_ATCC_35646 Bacillus thuringiensis serovar israelensis ATCC 35646]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KGK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.95Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4kgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgk OCA], [https://pdbe.org/4kgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kgk RCSB], [https://www.ebi.ac.uk/pdbsum/4kgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgk 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=4kgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgk OCA], [https://pdbe.org/4kgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kgk RCSB], [https://www.ebi.ac.uk/pdbsum/4kgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/Q3F0V8_BACTI Q3F0V8_BACTI]		[https://www.uniprot.org/uniprot/Q3F0V8_BACTI Q3F0V8_BACTI]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	All nucleotide polymerases and transferases catalyze nucleotide addition in a 5' to 3' direction. In contrast, tRNA(His) guanylyltransferase (Thg1) enzymes catalyze the unusual reverse addition (3' to 5') of nucleotides to polynucleotide substrates. In eukaryotes, Thg1 enzymes use the 3'-5' addition activity to add G-1 to the 5'-end of tRNA(His), a modification required for efficient aminoacylation of the tRNA by the histidyl-tRNA synthetase. Thg1-like proteins (TLPs) are found in Archaea, Bacteria, and mitochondria and are biochemically distinct from their eukaryotic Thg1 counterparts TLPs catalyze 5'-end repair of truncated tRNAs and act on a broad range of tRNA substrates instead of exhibiting strict specificity for tRNA(His). Taken together, these data suggest that TLPs function in distinct biological pathways from the tRNA(His) maturation pathway, perhaps in tRNA quality control. Here we present the first crystal structure of a TLP, from the gram-positive soil bacterium Bacillus thuringiensis (BtTLP). The enzyme is a tetramer like human THG1, with which it shares substantial structural similarity. Catalysis of the 3'-5' reaction with 5'-monophosphorylated tRNA necessitates first an activation step, generating a 5'-adenylylated intermediate prior to a second nucleotidyl transfer step, in which a nucleotide is transferred to the tRNA 5'-end. Consistent with earlier characterization of human THG1, we observed distinct binding sites for the nucleotides involved in these two steps of activation and nucleotidyl transfer. A BtTLP complex with GTP reveals new interactions with the GTP nucleotide in the activation site that were not evident from the previously solved structure. Moreover, the BtTLP-ATP structure allows direct observation of ATP in the activation site for the first time. The BtTLP structural data, combined with kinetic analysis of selected variants, provide new insight into the role of key residues in the activation step.
-
-	Structural Studies of a Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein, with Nucleotide in the Activation and Nucleotidyl Transfer Sites.,Hyde SJ, Rao BS, Eckenroth BE, Jackman JE, Doublie S PLoS One. 2013 Jul 3;8(7):e67465. doi: 10.1371/journal.pone.0067465. Print 2013. PMID:23844012<ref>PMID:23844012</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4kgk" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:57, 30 November 2022

OCA — Wed, 30 Nov 2022 11:57:45 GMT

←Older revision		Revision as of 11:57, 30 November 2022
Line 1:		Line 1:

	==Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP==		==Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP==
-	<StructureSection load='4kgk' size='340' side='right' caption='[[4kgk]], [[Resolution\|resolution]] 2.95Å' scene=''>	+	<StructureSection load='4kgk' size='340' side='right'caption='[[4kgk]], [[Resolution\|resolution]] 2.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4kgk]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Bacillus_thuringiensis_serovar_israelensis_atcc_35646~~ Bacillus thuringiensis serovar israelensis ~~atcc~~ 35646]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4KGK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4kgk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis_ATCC_35646 Bacillus thuringiensis serovar israelensis ATCC 35646]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KGK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4kgm\|4kgm]]</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=4kgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgk OCA], [https://pdbe.org/4kgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kgk RCSB], [https://www.ebi.ac.uk/pdbsum/4kgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgk ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBTH_06728 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=339854 Bacillus thuringiensis serovar israelensis ATCC 35646])</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=4kgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgk OCA], [~~http~~://pdbe.org/4kgk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4kgk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4kgk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgk ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q3F0V8_BACTI Q3F0V8_BACTI]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacillus thuringiensis serovar israelensis ~~atcc~~ 35646]]	+	[[Category: Bacillus thuringiensis serovar israelensis ATCC 35646]]
-	[[Category: ~~Doublie, S~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Eckenroth, B E]]~~	+	[[Category: Doublie S]]
-	~~[[Category: Hyde,~~ S J]]	+	[[Category: Eckenroth BE]]
-	[[Category: ~~Jackman, J E~~]]	+	[[Category: Hyde SJ]]
-	[[Category: ~~Rao, B S~~]]	+	[[Category: Jackman JE]]
-	[[Category: ~~Atp binding~~]]	+	[[Category: Rao BS]]
-	[[Category: ~~Gtp binding]]~~	+
-	~~[[Category: Polymerase-like catalytic domain]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Trna binding~~]]	+

OCA at 10:19, 11 August 2016

OCA — Thu, 11 Aug 2016 10:19:42 GMT

←Older revision		Revision as of 10:19, 11 August 2016
Line 1:		Line 1:
		+
	==Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP==		==Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP==
	<StructureSection load='4kgk' size='340' side='right' caption='[[4kgk]], [[Resolution\|resolution]] 2.95Å' scene=''>		<StructureSection load='4kgk' size='340' side='right' caption='[[4kgk]], [[Resolution\|resolution]] 2.95Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4kgm\|4kgm]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4kgm\|4kgm]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBTH_06728 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=339854 Bacillus thuringiensis serovar israelensis ATCC 35646])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBTH_06728 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=339854 Bacillus thuringiensis serovar israelensis ATCC 35646])</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=4kgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kgk RCSB], [http://www.ebi.ac.uk/pdbsum/4kgk 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=4kgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgk OCA], [http://pdbe.org/4kgk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kgk RCSB], [http://www.ebi.ac.uk/pdbsum/4kgk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgk ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	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 4kgk" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:31, 20 January 2015

OCA — Tue, 20 Jan 2015 11:31:56 GMT

←Older revision		Revision as of 11:31, 20 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4kgk\| PDB=4kgk \| SCENE= }}~~	+	==Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP==
-	===Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP===	+	<StructureSection load='4kgk' size='340' side='right' caption='[[4kgk]], [[Resolution\|resolution]] 2.95Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23844012}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4kgk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis_atcc_35646 Bacillus thuringiensis serovar israelensis atcc 35646]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KGK FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4kgm\|4kgm]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBTH_06728 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=339854 Bacillus thuringiensis serovar israelensis ATCC 35646])</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=4kgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kgk RCSB], [http://www.ebi.ac.uk/pdbsum/4kgk PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	All nucleotide polymerases and transferases catalyze nucleotide addition in a 5' to 3' direction. In contrast, tRNA(His) guanylyltransferase (Thg1) enzymes catalyze the unusual reverse addition (3' to 5') of nucleotides to polynucleotide substrates. In eukaryotes, Thg1 enzymes use the 3'-5' addition activity to add G-1 to the 5'-end of tRNA(His), a modification required for efficient aminoacylation of the tRNA by the histidyl-tRNA synthetase. Thg1-like proteins (TLPs) are found in Archaea, Bacteria, and mitochondria and are biochemically distinct from their eukaryotic Thg1 counterparts TLPs catalyze 5'-end repair of truncated tRNAs and act on a broad range of tRNA substrates instead of exhibiting strict specificity for tRNA(His). Taken together, these data suggest that TLPs function in distinct biological pathways from the tRNA(His) maturation pathway, perhaps in tRNA quality control. Here we present the first crystal structure of a TLP, from the gram-positive soil bacterium Bacillus thuringiensis (BtTLP). The enzyme is a tetramer like human THG1, with which it shares substantial structural similarity. Catalysis of the 3'-5' reaction with 5'-monophosphorylated tRNA necessitates first an activation step, generating a 5'-adenylylated intermediate prior to a second nucleotidyl transfer step, in which a nucleotide is transferred to the tRNA 5'-end. Consistent with earlier characterization of human THG1, we observed distinct binding sites for the nucleotides involved in these two steps of activation and nucleotidyl transfer. A BtTLP complex with GTP reveals new interactions with the GTP nucleotide in the activation site that were not evident from the previously solved structure. Moreover, the BtTLP-ATP structure allows direct observation of ATP in the activation site for the first time. The BtTLP structural data, combined with kinetic analysis of selected variants, provide new insight into the role of key residues in the activation step.

-	~~==About this Structure==~~	+	Structural Studies of a Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein, with Nucleotide in the Activation and Nucleotidyl Transfer Sites.,Hyde SJ, Rao BS, Eckenroth BE, Jackman JE, Doublie S PLoS One. 2013 Jul 3;8(7):e67465. doi: 10.1371/journal.pone.0067465. Print 2013. PMID:23844012<ref>PMID:23844012</ref>
-	~~[[4kgk]] is~~ a ~~4 chain structure~~ with ~~sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bacillus_thuringiensis_serovar_israelensis_atcc_35646 Bacillus thuringiensis serovar israelensis atcc 35646]~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=4KGK OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:023844012</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Bacillus thuringiensis serovar israelensis atcc 35646]]		[[Category: Bacillus thuringiensis serovar israelensis atcc 35646]]
-	[[Category: Doublie, S.]]	+	[[Category: Doublie, S]]
-	[[Category: Eckenroth, B E.]]	+	[[Category: Eckenroth, B E]]
-	[[Category: Hyde, S J.]]	+	[[Category: Hyde, S J]]
-	[[Category: Jackman, J E.]]	+	[[Category: Jackman, J E]]
-	[[Category: Rao, B S.]]	+	[[Category: Rao, B S]]
	[[Category: Atp binding]]		[[Category: Atp binding]]
	[[Category: Gtp binding]]		[[Category: Gtp binding]]

OCA at 07:49, 14 August 2013

OCA — Wed, 14 Aug 2013 07:49:47 GMT

←Older revision		Revision as of 07:49, 14 August 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4kgk\| PDB=4kgk \| SCENE= }}
		+	===Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP===
		+	{{ABSTRACT_PUBMED_23844012}}

-	~~The entry~~ 4kgk is ~~ON HOLD until Paper Publication~~	+	==About this Structure==
		+	[[4kgk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis_atcc_35646 Bacillus thuringiensis serovar israelensis atcc 35646]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGK OCA].

-	~~Authors~~: ~~Hyde~~, S.~~J., Rao, B.S.,~~ Eckenroth, B.E., Jackman, J.E., ~~Doublie,~~ S.	+	==Reference==
-		+	<ref group="xtra">PMID:023844012</ref><references group="xtra"/><references/>
-	~~Description~~: ~~Crystal structure of a bacterial enzyme~~	+	[[Category: Bacillus thuringiensis serovar israelensis atcc 35646]]
		+	[[Category: Doublie, S.]]
		+	[[Category: Eckenroth, B E.]]
		+	[[Category: Hyde, S J.]]
		+	[[Category: Jackman, J E.]]
		+	[[Category: Rao, B S.]]
		+	[[Category: Atp binding]]
		+	[[Category: Gtp binding]]
		+	[[Category: Polymerase-like catalytic domain]]
		+	[[Category: Transferase]]
		+	[[Category: Trna binding]]

OCA at 13:11, 3 July 2013

OCA — Wed, 03 Jul 2013 13:11:45 GMT

←Older revision		Revision as of 13:11, 3 July 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4kgk is ON HOLD	+	The entry 4kgk is ON HOLD until Paper Publication

	Authors: Hyde, S.J., Rao, B.S., Eckenroth, B.E., Jackman, J.E., Doublie, S.		Authors: Hyde, S.J., Rao, B.S., Eckenroth, B.E., Jackman, J.E., Doublie, S.

	Description: Crystal structure of a bacterial enzyme		Description: Crystal structure of a bacterial enzyme

OCA: Protected "4kgk" [edit=sysop:move=sysop]

OCA — Wed, 08 May 2013 07:22:51 GMT

Protected "4kgk" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:22, 8 May 2013

OCA: New page: '''Unreleased structure''' The entry 4kgk is ON HOLD Authors: Hyde, S.J., Rao, B.S., Eckenroth, B.E., Jackman, J.E., Doublie, S. Description: Crystal structure of a bacterial enzyme

OCA — Wed, 08 May 2013 07:22:50 GMT

New page: '''Unreleased structure''' The entry 4kgk is ON HOLD Authors: Hyde, S.J., Rao, B.S., Eckenroth, B.E., Jackman, J.E., Doublie, S. Description: Crystal structure of a bacterial enzyme

New page

'''Unreleased structure'''

The entry 4kgk is ON HOLD

Authors: Hyde, S.J., Rao, B.S., Eckenroth, B.E., Jackman, J.E., Doublie, S.

Description: Crystal structure of a bacterial enzyme