1eks - Revision history

OCA at 07:04, 7 February 2024

2024-02-07T07:04:01Z

← Older revision		Revision as of 07:04, 7 February 2024
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	<StructureSection load='1eks' size='340' side='right'caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1eks' size='340' side='right'caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EKS FirstGlance]. <br>		<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EKS FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=TLA:L(+)~~-~~TARTARIC+ACID'>TLA</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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1ekr\|1ekr]]~~</~~div~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [https://pdbe.org/1eks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [https://www.ebi.ac.uk/pdbsum/1eks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eks 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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [https://pdbe.org/1eks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [https://www.ebi.ac.uk/pdbsum/1eks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eks ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/MOAC_ECOLI MOAC_ECOLI]] Together with MoaA, is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).[HAMAP-Rule:MF_01224_B]		[https://www.uniprot.org/uniprot/MOAC_ECOLI MOAC_ECOLI] Together with MoaA, is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).[HAMAP-Rule:MF_01224_B]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eks ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eks ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	BACKGROUND: The molybdenum cofactor (Moco) is an essential component of a large family of enzymes involved in important transformations in carbon, nitrogen and sulfur metabolism. The Moco biosynthetic pathway is evolutionarily conserved and found in archaea, eubacteria and eukaryotes. In humans, genetic deficiencies of enzymes involved in this pathway trigger an autosomal recessive and usually deadly disease with severe neurological symptoms. The MoaC protein, together with the MoaA protein, is involved in the first step of Moco biosynthesis. RESULTS: MoaC from Escherichia coli has been expressed and purified to homogeneity and its crystal structure determined at 2 A resolution. The enzyme is organized into a tightly packed hexamer with 32 symmetry. The monomer consists of an antiparallel, four-stranded beta sheet packed against two long alpha helices, and its fold belongs to the ferredoxin-like family. Analysis of structural and biochemical data strongly suggests that the active site is located at the interface of two monomers in a pocket that contains several strictly conserved residues. CONCLUSIONS: Asp128 in the putative active site appears to be important for catalysis as its replacement with alanine almost completely abolishes protein activity. The structure of the Asp128-->Ala variant reveals substantial conformational changes in an adjacent loop. In the human MoaC ortholog, substitution of Thr182 with proline causes Moco deficiency, and the corresponding substitution in MoaC severely compromises activity. This residue is located near the N-terminal end of helix alpha4 at an interface between two monomers. The MoaC structure provides a framework for the analysis of additional dysfunctional mutations in the corresponding human gene.

	Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC.,Wuebbens MM, Liu MT, Rajagopalan K, Schindelin H Structure. 2000 Jul 15;8(7):709-18. PMID:10903949<ref>PMID:10903949</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 1eks" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]		[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Liu~~, M T.W~~]]		[[Category: Liu MTW]]
	[[Category: Rajagopalan~~, K V~~]]		[[Category: Rajagopalan KV]]
	[[Category: Schindelin, H]]		[[Category: Schindelin H]]
	[[Category: Wuebbens~~, M M]]~~		[[Category: Wuebbens MM]]
	~~[[Category: Moac]]~~
	~~[[Category: Moco biosynthesis]]~~
	~~[[Category: Moco deficiency]]~~
	~~[[Category: Translation~~]]

OCA at 06:32, 11 August 2021

2021-08-11T06:32:15Z

← Older revision		Revision as of 06:32, 11 August 2021
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	<StructureSection load='1eks' size='340' side='right'caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1eks' size='340' side='right'caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1EKS FirstGlance]. <br>		<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EKS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekr\|1ekr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ekr\|1ekr]]</div></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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [~~http~~://pdbe.org/1eks PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1eks PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1eks 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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [https://pdbe.org/1eks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [https://www.ebi.ac.uk/pdbsum/1eks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eks ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/MOAC_ECOLI MOAC_ECOLI]] Together with MoaA, is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).[HAMAP-Rule:MF_01224_B]		[[https://www.uniprot.org/uniprot/MOAC_ECOLI MOAC_ECOLI]] Together with MoaA, is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).[HAMAP-Rule:MF_01224_B]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:33, 6 November 2019

2019-11-06T09:33:38Z

← Older revision		Revision as of 09:33, 6 November 2019
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	==ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI==		==ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI==
	<StructureSection load='1eks' size='340' side='right' caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1eks' size='340' side='right'caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EKS FirstGlance]. <br>		<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EKS FirstGlance]. <br>
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	</StructureSection>		</StructureSection>
	[[Category: Bacillus coli migula 1895]]		[[Category: Bacillus coli migula 1895]]
			[[Category: Large Structures]]
	[[Category: Liu, M T.W]]		[[Category: Liu, M T.W]]
	[[Category: Rajagopalan, K V]]		[[Category: Rajagopalan, K V]]

OCA at 07:10, 20 December 2017

2017-12-20T07:10:27Z

← Older revision		Revision as of 07:10, 20 December 2017
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	==ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI==		==ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI==
	<StructureSection load='1eks' size='340' side='right' caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1eks' size='340' side='right' caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekr\|1ekr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekr\|1ekr]]</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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [http://pdbe.org/1eks PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [http://www.ebi.ac.uk/pdbsum/1eks 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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [http://pdbe.org/1eks PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [http://www.ebi.ac.uk/pdbsum/1eks PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eks ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ek/1eks_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ek/1eks_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 01:33, 9 February 2016

2016-02-09T01:33:01Z

← Older revision		Revision as of 01:33, 9 February 2016
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eks ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 17:19, 10 September 2015

2015-09-10T17:19:06Z

← Older revision		Revision as of 17:19, 10 September 2015
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	<StructureSection load='1eks' size='340' side='right' caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1eks' size='340' side='right' caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence 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=1EKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EKS FirstGlance]. <br>		<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EKS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekr\|1ekr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekr\|1ekr]]</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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [http://www.ebi.ac.uk/pdbsum/1eks 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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [http://pdbe.org/1eks PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [http://www.ebi.ac.uk/pdbsum/1eks PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 1eks" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Escherichia~~ coli]]		[[Category: Bacillus coli migula 1895]]
	[[Category: Liu, M T.W]]		[[Category: Liu, M T.W]]
	[[Category: Rajagopalan, K V]]		[[Category: Rajagopalan, K V]]

OCA at 03:30, 25 December 2014

2014-12-25T03:30:55Z

← Older revision		Revision as of 03:30, 25 December 2014
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	<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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [http://www.ebi.ac.uk/pdbsum/1eks 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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [http://www.ebi.ac.uk/pdbsum/1eks PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/MOAC_ECOLI MOAC_ECOLI]] Together with MoaA, is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).[HAMAP-Rule:MF_01224_B]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 19:46, 22 December 2014

2014-12-22T19:46:09Z

← Older revision		Revision as of 19:46, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence 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=1EKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EKS FirstGlance]. <br>		<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence 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=1EKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EKS FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekr\|1ekr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekr\|1ekr]]</td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [http://www.ebi.ac.uk/pdbsum/1eks 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=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [http://www.ebi.ac.uk/pdbsum/1eks PDBsum]</span></td></tr>
	<table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Liu, M T.W.]]		[[Category: Liu, M T.W]]
	[[Category: Rajagopalan, K V.]]		[[Category: Rajagopalan, K V]]
	[[Category: Schindelin, H.]]		[[Category: Schindelin, H]]
	[[Category: Wuebbens, M M.]]		[[Category: Wuebbens, M M]]
	[[Category: Moac]]		[[Category: Moac]]
	[[Category: Moco biosynthesis]]		[[Category: Moco biosynthesis]]
	[[Category: Moco deficiency]]		[[Category: Moco deficiency]]
	[[Category: Translation]]		[[Category: Translation]]

OCA at 11:21, 24 September 2014

2014-09-24T11:21:13Z

← Older revision		Revision as of 11:21, 24 September 2014
Line 1:		Line 1:
	[[Image:~~1eks~~.~~png~~\|~~left~~\|~~200px~~]]		==ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI==
			<StructureSection load='1eks' size='340' side='right' caption='[[1eks]], [[Resolution\|resolution]] 2.50Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[1eks]] is a 1 chain structure with sequence 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=1EKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EKS FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekr\|1ekr]]</td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eks OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eks RCSB], [http://www.ebi.ac.uk/pdbsum/1eks PDBsum]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ek/1eks_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			BACKGROUND: The molybdenum cofactor (Moco) is an essential component of a large family of enzymes involved in important transformations in carbon, nitrogen and sulfur metabolism. The Moco biosynthetic pathway is evolutionarily conserved and found in archaea, eubacteria and eukaryotes. In humans, genetic deficiencies of enzymes involved in this pathway trigger an autosomal recessive and usually deadly disease with severe neurological symptoms. The MoaC protein, together with the MoaA protein, is involved in the first step of Moco biosynthesis. RESULTS: MoaC from Escherichia coli has been expressed and purified to homogeneity and its crystal structure determined at 2 A resolution. The enzyme is organized into a tightly packed hexamer with 32 symmetry. The monomer consists of an antiparallel, four-stranded beta sheet packed against two long alpha helices, and its fold belongs to the ferredoxin-like family. Analysis of structural and biochemical data strongly suggests that the active site is located at the interface of two monomers in a pocket that contains several strictly conserved residues. CONCLUSIONS: Asp128 in the putative active site appears to be important for catalysis as its replacement with alanine almost completely abolishes protein activity. The structure of the Asp128-->Ala variant reveals substantial conformational changes in an adjacent loop. In the human MoaC ortholog, substitution of Thr182 with proline causes Moco deficiency, and the corresponding substitution in MoaC severely compromises activity. This residue is located near the N-terminal end of helix alpha4 at an interface between two monomers. The MoaC structure provides a framework for the analysis of additional dysfunctional mutations in the corresponding human gene.

	~~{{STRUCTURE_1eks\| PDB=1eks \| SCENE= }}~~		Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC.,Wuebbens MM, Liu MT, Rajagopalan K, Schindelin H Structure. 2000 Jul 15;8(7):709-18. PMID:10903949<ref>PMID:10903949</ref>

	~~===ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			== References ==
	~~==About this Structure==~~		<references/>
	~~[[1eks]] is~~ a ~~1 chain structure with sequence 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=1EKS OCA].~~		__TOC__
			</StructureSection>
	==~~Reference~~==
	<~~ref group="xtra">PMID:010903949<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Liu, M T.W.]]		[[Category: Liu, M T.W.]]

OCA: Protected "1eks" [edit=sysop:move=sysop]

2012-11-08T14:29:23Z

Protected "1eks" [edit=sysop:move=sysop]

← Older revision	Revision as of 14:29, 8 November 2012
(No difference)