2k7v

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[[Image:2k7v.png|left|200px]]
 
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{{STRUCTURE_2k7v| PDB=2k7v | SCENE= }}
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==Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form==
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<StructureSection load='2k7v' size='340' side='right'caption='[[2k7v]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2k7v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K7V FirstGlance]. <br>
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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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7v OCA], [https://pdbe.org/2k7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k7v RCSB], [https://www.ebi.ac.uk/pdbsum/2k7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ODP2_ECOLI ODP2_ECOLI] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/2k7v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2k7v ConSurf].
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<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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A prominent surface loop links the first two beta strands of the lipoyl domain (E2plip) from the pyruvate dehydrogenase multienzyme complex of Escherichia coli. We show here that shortening this loop by two residues generates a protein that populates two structurally distinct stable conformers: an active, native-like monomer (HM) and a functionally compromised misfolded dimer (LM). Conversion of LM to HM was observed after exposure to temperatures above 50 degrees C. Removal of two additional residues from the loop caused the protein to adopt exclusively the misfolded conformation. Detailed NMR structural studies of the misfolded dimer reveal that the N-terminal half of the domain was unfolded and dynamic, whereas the C-terminal halves of two monomers had associated to form a structure with two-fold symmetry and a topology mimicking that of the folded monomer. The surface loop is therefore a hitherto unsuspected determinant in the folding process that leads to a functional protein.
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===Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form===
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A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure.,Stott KM, Yusof AM, Perham RN, Jones DD Structure. 2009 Aug 12;17(8):1117-27. PMID:19679089<ref>PMID:19679089</ref>
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{{ABSTRACT_PUBMED_19679089}}
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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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==About this Structure==
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<div class="pdbe-citations 2k7v" style="background-color:#fffaf0;"></div>
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[[2k7v]] is a 2 chain structure of [[Dihydrolipoamide acetyltransferase]] and [[Pyruvate dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7V OCA].
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==See Also==
==See Also==
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*[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]]
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*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
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*[[Pyruvate dehydrogenase|Pyruvate dehydrogenase]]
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:019679089</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Jones, D D.]]
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[[Category: Jones DD]]
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[[Category: Perham, R N.]]
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[[Category: Perham RN]]
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[[Category: Stott, K M.]]
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[[Category: Stott KM]]
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[[Category: Yusof, A M.]]
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[[Category: Yusof AM]]
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[[Category: Acyltransferase]]
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[[Category: Glycolysis]]
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[[Category: Lipoyl]]
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[[Category: Misfolded dimer]]
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[[Category: Transferase]]
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Current revision

Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form

PDB ID 2k7v

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