1rwu

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==Solution structure of conserved protein YbeD from E. coli==
==Solution structure of conserved protein YbeD from E. coli==
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<StructureSection load='1rwu' size='340' side='right'caption='[[1rwu]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
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<StructureSection load='1rwu' size='340' side='right'caption='[[1rwu]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1rwu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RWU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1rwu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RWU FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YBED, B0631, C0721, Z0776, ECS0669, SF0650, S0672 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1rwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rwu OCA], [https://pdbe.org/1rwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rwu RCSB], [https://www.ebi.ac.uk/pdbsum/1rwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rwu ProSAT], [https://www.topsan.org/Proteins/NESGC/1rwu TOPSAN]</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=1rwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rwu OCA], [https://pdbe.org/1rwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rwu RCSB], [https://www.ebi.ac.uk/pdbsum/1rwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rwu ProSAT], [https://www.topsan.org/Proteins/NESGC/1rwu TOPSAN]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/YBED_ECOLI YBED_ECOLI]
== 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=1rwu 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=1rwu ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Lipoic acid is an essential prosthetic group in several metabolic pathways. The biosynthetic pathway of protein lipoylation in Escherichia coli involves gene products of the lip operon. YbeD is a conserved bacterial protein located in the dacA-lipB intergenic region. Here, we report the nuclear magnetic resonance structure of YbeD from E. coli. The structure includes a beta alpha beta beta alpha beta fold with two alpha-helices on one side of a four-strand antiparallel beta-sheet. The beta 2-beta 3 loop shows the highest sequence conservation and is likely functionally important. The beta-sheet surface contains a patch of conserved hydrophobic residues, suggesting a role in protein-protein interactions. YbeD shows striking structural homology to the regulatory domain from d-3-phosphoglycerate dehydrogenase, hinting at a role in the allosteric regulation of lipoic acid biosynthesis or the glycine cleavage system.
 
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Structural similarity of YbeD protein from Escherichia coli to allosteric regulatory domains.,Kozlov G, Elias D, Semesi A, Yee A, Cygler M, Gehring K J Bacteriol. 2004 Dec;186(23):8083-8. PMID:15547281<ref>PMID:15547281</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1rwu" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Gehring, K]]
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[[Category: Gehring K]]
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[[Category: Kozlov, G]]
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[[Category: Kozlov G]]
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[[Category: Structural genomic]]
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[[Category: Mixed alpha-beta fold]]
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[[Category: Nesg]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Unknown function]]
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Revision as of 08:27, 1 May 2024

Solution structure of conserved protein YbeD from E. coli

PDB ID 1rwu

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