3pbk - Revision history

OCA at 09:50, 6 September 2023

OCA — Wed, 06 Sep 2023 09:50:59 GMT

←Older revision		Revision as of 09:50, 6 September 2023
Line 1:		Line 1:

	==Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila==		==Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila==
-	<StructureSection load='3pbk' size='340' side='right'caption='[[3pbk]]' scene=''>	+	<StructureSection load='3pbk' size='340' side='right'caption='[[3pbk]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqw 3gqw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PBK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3pbk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O6 Escherichia coli O6]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqw 3gqw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PBK FirstGlance]. <br>
-	</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=3pbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbk OCA], [https://pdbe.org/3pbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pbk RCSB], [https://www.ebi.ac.uk/pdbsum/3pbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pbk ProSAT]</span></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]] 3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1ZZ:5-O-[(S)-(DODECANOYLOXY)(HYDROXY)PHOSPHORYL]ADENOSINE'>1ZZ</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3pbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbk OCA], [https://pdbe.org/3pbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pbk RCSB], [https://www.ebi.ac.uk/pdbsum/3pbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pbk ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/A0A0H2VDD9_ECOL6 A0A0H2VDD9_ECOL6]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Fatty acyl-AMP ligase (FAAL) is a new member of a family of adenylate-forming enzymes that were recently discovered in Mycobacterium tuberculosis. They are similar in sequence to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, while FACLs perform a two-step catalytic reaction, AMP ligation followed by CoA ligation using ATP and CoA as cofactors, FAALs produce only the acyl adenylate and are unable to perform the second step. We report X-ray crystal structures of full-length FAAL from Escherichia coli (EcFAAL) and FAAL from Legionella pneumophila (LpFAAL) bound to acyl adenylate, determined at resolution limits of 3.0 and 1.85 A, respectively. The structures share a larger N-terminal domain and a smaller C-terminal domain, which together resemble the previously determined structures of FAAL and FACL proteins. Our two structures occur in quite different conformations. EcFAAL adopts the adenylate-forming conformation typical of FACLs, whereas LpFAAL exhibits a unique intermediate conformation. Both EcFAAL and LpFAAL have insertion motifs that distinguish them from the FACLs. Structures of EcFAAL and LpFAAL reveal detailed interactions between this insertion motif and the interdomain hinge region and with the C-terminal domain. We suggest that the insertion motifs support sufficient interdomain motions to allow substrate binding and product release during acyl adenylate formation, but they preclude CoA binding, thereby preventing CoA ligation.
		+
		+	Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila.,Zhang Z, Zhou R, Sauder JM, Tonge PJ, Burley SK, Swaminathan S J Mol Biol. 2010 Dec 23. PMID:21185305<ref>PMID:21185305</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 3pbk" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Escherichia coli O6]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Burley SK]]		[[Category: Burley SK]]
	[[Category: Swaminathan S]]		[[Category: Swaminathan S]]
	[[Category: Zhang Z]]		[[Category: Zhang Z]]

OCA at 08:32, 25 May 2022

OCA — Wed, 25 May 2022 08:32:48 GMT

←Older revision		Revision as of 08:32, 25 May 2022
Line 1:		Line 1:

	==Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila==		==Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila==
-	<StructureSection load='3pbk' size='340' side='right' caption='[[3pbk]]~~, [[Resolution\|resolution]] 3.00Å~~' scene=''>	+	<StructureSection load='3pbk' size='340' side='right'caption='[[3pbk]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[3pbk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o6 Escherichia coli o6].~~ This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqw 3gqw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3PBK FirstGlance]. <br>	+	<table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqw 3gqw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PBK FirstGlance]. <br>
-	</td></tr>~~<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1ZZ:5-O-[(S)-(DODECANOYLOXY)(HYDROXY)PHOSPHORYL]ADENOSINE'>1ZZ</scene></td></tr>~~	+	</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=3pbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbk OCA], [https://pdbe.org/3pbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pbk RCSB], [https://www.ebi.ac.uk/pdbsum/3pbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pbk ProSAT]</span></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">c3712 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=217992 Escherichia coli O6])</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=3pbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbk OCA], [~~http~~://pdbe.org/3pbk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3pbk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3pbk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3pbk ProSAT]</span></td></tr>	+
	</table>		</table>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Fatty acyl-AMP ligase (FAAL) is a new member of a family of adenylate-forming enzymes that were recently discovered in Mycobacterium tuberculosis. They are similar in sequence to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, while FACLs perform a two-step catalytic reaction, AMP ligation followed by CoA ligation using ATP and CoA as cofactors, FAALs produce only the acyl adenylate and are unable to perform the second step. We report X-ray crystal structures of full-length FAAL from Escherichia coli (EcFAAL) and FAAL from Legionella pneumophila (LpFAAL) bound to acyl adenylate, determined at resolution limits of 3.0 and 1.85 A, respectively. The structures share a larger N-terminal domain and a smaller C-terminal domain, which together resemble the previously determined structures of FAAL and FACL proteins. Our two structures occur in quite different conformations. EcFAAL adopts the adenylate-forming conformation typical of FACLs, whereas LpFAAL exhibits a unique intermediate conformation. Both EcFAAL and LpFAAL have insertion motifs that distinguish them from the FACLs. Structures of EcFAAL and LpFAAL reveal detailed interactions between this insertion motif and the interdomain hinge region and with the C-terminal domain. We suggest that the insertion motifs support sufficient interdomain motions to allow substrate binding and product release during acyl adenylate formation, but they preclude CoA binding, thereby preventing CoA ligation.
-
-	Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila.,Zhang Z, Zhou R, Sauder JM, Tonge PJ, Burley SK, Swaminathan S J Mol Biol. 2010 Dec 23. PMID:21185305<ref>PMID:21185305</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3pbk" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli o6~~]]	+	[[Category: Large Structures]]
-	[[Category: Burley~~, S K]]~~	+	[[Category: Burley SK]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Swaminathan S]]
-	[[Category: Swaminathan, S]]	+	[[Category: Zhang Z]]
-	[[Category: Zhang, Z]]	+
-	~~[[Category: Atp-dependent amp-binding enzyme family]]~~	+
-	~~[[Category: Faal]]~~	+
-	~~[[Category: Fatty acid amp ligase]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]~~	+
-	~~[[Category: PSI, Protein structure initiative~~]]	+

OCA at 12:19, 11 August 2016

OCA — Thu, 11 Aug 2016 12:19:11 GMT

←Older revision		Revision as of 12:19, 11 August 2016
Line 1:		Line 1:
		+
	==Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila==		==Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila==
	<StructureSection load='3pbk' size='340' side='right' caption='[[3pbk]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='3pbk' size='340' side='right' caption='[[3pbk]], [[Resolution\|resolution]] 3.00Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">c3712 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=217992 Escherichia coli O6])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">c3712 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=217992 Escherichia coli O6])</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=3pbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pbk RCSB], [http://www.ebi.ac.uk/pdbsum/3pbk 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=3pbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbk OCA], [http://pdbe.org/3pbk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pbk RCSB], [http://www.ebi.ac.uk/pdbsum/3pbk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pbk 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 3pbk" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:53, 6 November 2014

OCA — Thu, 06 Nov 2014 13:53:48 GMT

←Older revision		Revision as of 13:53, 6 November 2014
Line 1:		Line 1:
-	[[~~Image:~~3pbk.~~png~~\|~~left~~\|~~200px~~]]	+	==Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila==
		+	<StructureSection load='3pbk' size='340' side='right' caption='[[3pbk]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3pbk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o6 Escherichia coli o6]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqw 3gqw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PBK FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1ZZ:5-O-[(S)-(DODECANOYLOXY)(HYDROXY)PHOSPHORYL]ADENOSINE'>1ZZ</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">c3712 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=217992 Escherichia coli O6])</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=3pbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pbk RCSB], [http://www.ebi.ac.uk/pdbsum/3pbk PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Fatty acyl-AMP ligase (FAAL) is a new member of a family of adenylate-forming enzymes that were recently discovered in Mycobacterium tuberculosis. They are similar in sequence to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, while FACLs perform a two-step catalytic reaction, AMP ligation followed by CoA ligation using ATP and CoA as cofactors, FAALs produce only the acyl adenylate and are unable to perform the second step. We report X-ray crystal structures of full-length FAAL from Escherichia coli (EcFAAL) and FAAL from Legionella pneumophila (LpFAAL) bound to acyl adenylate, determined at resolution limits of 3.0 and 1.85 A, respectively. The structures share a larger N-terminal domain and a smaller C-terminal domain, which together resemble the previously determined structures of FAAL and FACL proteins. Our two structures occur in quite different conformations. EcFAAL adopts the adenylate-forming conformation typical of FACLs, whereas LpFAAL exhibits a unique intermediate conformation. Both EcFAAL and LpFAAL have insertion motifs that distinguish them from the FACLs. Structures of EcFAAL and LpFAAL reveal detailed interactions between this insertion motif and the interdomain hinge region and with the C-terminal domain. We suggest that the insertion motifs support sufficient interdomain motions to allow substrate binding and product release during acyl adenylate formation, but they preclude CoA binding, thereby preventing CoA ligation.

-	~~{{STRUCTURE_3pbk\| PDB=3pbk \| SCENE= }}~~	+	Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila.,Zhang Z, Zhou R, Sauder JM, Tonge PJ, Burley SK, Swaminathan S J Mol Biol. 2010 Dec 23. PMID:21185305<ref>PMID:21185305</ref>

-	~~===Structural and Functional Studies~~ of ~~Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_21185305}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[3pbk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o6 Escherichia coli o6]. This structure supersedes~~ the ~~now removed PDB entry [http://oca~~.~~weizmann~~.ac.il/~~oca-bin/send-pdb?obs=1&id=3gqw 3gqw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:021185305<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Escherichia coli o6]]		[[Category: Escherichia coli o6]]
-	[[Category: Burley, S K.]]	+	[[Category: Burley, S K]]
-	[[Category: ~~NYSGXRC, New York SGX Research Center for~~ Structural ~~Genomics.~~]]	+	[[Category: Structural genomic]]
-	[[Category: Swaminathan, S.]]	+	[[Category: Swaminathan, S]]
-	[[Category: Zhang, Z.]]	+	[[Category: Zhang, Z]]
	[[Category: Atp-dependent amp-binding enzyme family]]		[[Category: Atp-dependent amp-binding enzyme family]]
	[[Category: Faal]]		[[Category: Faal]]
	[[Category: Fatty acid amp ligase]]		[[Category: Fatty acid amp ligase]]
	[[Category: Ligase]]		[[Category: Ligase]]
-	[[Category: New ~~york sgx research center~~ for ~~structural genomic]]~~	+	[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
-	~~[[Category: Nysgxrc~~]]	+	[[Category: PSI, Protein structure initiative]]
-	[[Category: Protein structure initiative]]	+
-	~~[[Category: Psi-2]]~~	+
-	~~[[Category: Structural genomic~~]]	+

OCA at 10:36, 19 December 2012

OCA — Wed, 19 Dec 2012 10:36:31 GMT

←Older revision		Revision as of 10:36, 19 December 2012
Line 1:		Line 1:
	[[Image:3pbk.png\|left\|200px]]		[[Image:3pbk.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3pbk", creates the "Structure Box" on the page.
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	{{STRUCTURE_3pbk\| PDB=3pbk \| SCENE= }}		{{STRUCTURE_3pbk\| PDB=3pbk \| SCENE= }}

	===Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila===		===Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila===

-
-	<!--
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-	(as it appears on PubMed at http://www.pubmed.gov), where 21185305 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_21185305}}		{{ABSTRACT_PUBMED_21185305}}

	==About this Structure==		==About this Structure==
-	[[3pbk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli~~ Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqw 3gqw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA].	+	[[3pbk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o6 Escherichia coli o6]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqw 3gqw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~21185305~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021185305</ref><references group="xtra"/>
-	[[Category: Escherichia coli]]	+	[[Category: Escherichia coli o6]]
	[[Category: Burley, S K.]]		[[Category: Burley, S K.]]
	[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics.]]		[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics.]]
	[[Category: Swaminathan, S.]]		[[Category: Swaminathan, S.]]
	[[Category: Zhang, Z.]]		[[Category: Zhang, Z.]]
		+	[[Category: Atp-dependent amp-binding enzyme family]]
		+	[[Category: Faal]]
		+	[[Category: Fatty acid amp ligase]]
		+	[[Category: Ligase]]
		+	[[Category: New york sgx research center for structural genomic]]
		+	[[Category: Nysgxrc]]
		+	[[Category: Protein structure initiative]]
		+	[[Category: Psi-2]]
		+	[[Category: Structural genomic]]

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

OCA — Wed, 23 Feb 2011 09:20:42 GMT

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

←Older revision

Revision as of 09:20, 23 February 2011

OCA at 09:20, 23 February 2011

OCA — Wed, 23 Feb 2011 09:20:40 GMT

←Older revision		Revision as of 09:20, 23 February 2011
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3pbk.png\|left\|200px]]
-	[[Image:3pbk.~~jpg~~\|left\|200px]]	+

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	===Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila===		===Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21185305}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21185305 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21185305}}

	==About this Structure==		==About this Structure==
-	~~3PBK~~ is a 2 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA].	+	[[3pbk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqw 3gqw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:21185305</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Burley, S K.]]		[[Category: Burley, S K.]]
Line 20:		Line 28:
	[[Category: Swaminathan, S.]]		[[Category: Swaminathan, S.]]
	[[Category: Zhang, Z.]]		[[Category: Zhang, Z.]]
-	[[Category: Atp-dependent amp-binding enzyme family]]
-	[[Category: Faal]]
-	[[Category: Fatty acid amp ligase]]
-	[[Category: Ligase]]
-	[[Category: New york sgx research center for structural genomic]]
-	[[Category: Nysgxrc]]
-	[[Category: Protein structure initiative]]
-	[[Category: Psi-2]]
-	[[Category: Structural genomic]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 10:04:29 2010''

OCA at 06:51, 22 December 2010

OCA — Wed, 22 Dec 2010 06:51:53 GMT

←Older revision		Revision as of 06:51, 22 December 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3pbk.jpg\|left\|200px]]

-	The ~~entry 3pbk~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3pbk", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3pbk\| PDB=3pbk \| SCENE= }}

-	~~Authors: Zhang, Z~~.~~, Burley, S~~.~~K., Swaminathan, S., New York SGX Research Center for Structural Genomics (NYSGXRC)~~	+	===Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila===

-	Description: Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec ~~15 08~~:23:19 2010''	+	==About this Structure==
		+	3PBK is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBK OCA].
		+	[[Category: Escherichia coli]]
		+	[[Category: Burley, S K.]]
		+	[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics.]]
		+	[[Category: Swaminathan, S.]]
		+	[[Category: Zhang, Z.]]
		+	[[Category: Atp-dependent amp-binding enzyme family]]
		+	[[Category: Faal]]
		+	[[Category: Fatty acid amp ligase]]
		+	[[Category: Ligase]]
		+	[[Category: New york sgx research center for structural genomic]]
		+	[[Category: Nysgxrc]]
		+	[[Category: Protein structure initiative]]
		+	[[Category: Psi-2]]
		+	[[Category: Structural genomic]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 10:04:29 2010''

OCA at 05:10, 15 December 2010

OCA — Wed, 15 Dec 2010 05:10:59 GMT

←Older revision		Revision as of 05:10, 15 December 2010
Line 3:		Line 3:
	The entry 3pbk is ON HOLD		The entry 3pbk is ON HOLD

-	Authors: Zhang, Z., Burley, S. K, Swaminathan, S., New York SGX Research Center for Structural Genomics (NYSGXRC)	+	Authors: Zhang, Z., Burley, S.K., Swaminathan, S., New York SGX Research Center for Structural Genomics (NYSGXRC)

	Description: Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila		Description: Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Nov 3 10~~:07:11 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 15 08:23:19 2010''

OCA: New page: '''Unreleased structure''' The entry 3pbk is ON HOLD Authors: Zhang, Z., Burley, S. K, Swaminathan, S., New York SGX Research Center for Structural Genomics (NYSGXRC) Description: Stru...

OCA — Wed, 03 Nov 2010 06:56:32 GMT

New page: '''Unreleased structure''' The entry 3pbk is ON HOLD Authors: Zhang, Z., Burley, S. K, Swaminathan, S., New York SGX Research Center for Structural Genomics (NYSGXRC) Description: Stru...

New page

'''Unreleased structure'''

The entry 3pbk is ON HOLD

Authors: Zhang, Z., Burley, S. K, Swaminathan, S., New York SGX Research Center for Structural Genomics (NYSGXRC)

Description: Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 3 10:07:11 2010''