2k7v

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[[Image:2k7v.png|left|200px]]
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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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' 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 [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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K7V FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aceF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr>
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<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=2k7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k7v RCSB], [http://www.ebi.ac.uk/pdbsum/2k7v PDBsum]</span></td></tr>
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<table>
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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/chain_selection.php?pdb_ID=2ata 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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{{STRUCTURE_2k7v| PDB=2k7v | SCENE= }}
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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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===Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form===
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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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{{ABSTRACT_PUBMED_19679089}}
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==About this Structure==
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[[2k7v]] is a 2 chain structure 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==
*[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]]
*[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]]
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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>
[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]

Revision as of 02:20, 29 September 2014

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

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