2ii5: Difference between revisions

Revision as of 17:15, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ii5.png

Template:STRUCTURE 2ii5

Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (E2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), Isobutyryl-Coenzyme A-bound formCrystal structure of a cubic core of the dihydrolipoamide acyltransferase (E2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), Isobutyryl-Coenzyme A-bound form

Template:ABSTRACT PUBMED 17124494

About this StructureAbout this Structure

2II5 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complex., Kato M, Wynn RM, Chuang JL, Brautigam CA, Custorio M, Chuang DT, EMBO J. 2006 Dec 13;25(24):5983-94. Epub 2006 Nov 23. PMID:17124494

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OCA

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 {{STRUCTURE_2ii5|  PDB=2ii5  |  SCENE=  }}
-'''Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (E2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), Isobutyryl-Coenzyme A-bound form'''
+===Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (E2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), Isobutyryl-Coenzyme A-bound form===
-==Overview==
+<!--
-The dihydrolipoamide acyltransferase (E2b) component of the branched-chain alpha-ketoacid dehydrogenase complex forms a cubic scaffold that catalyzes acyltransfer from S-acyldihydrolipoamide to CoA to produce acyl-CoA. We have determined the first crystal structures of a mammalian (bovine) E2b core domain with and without a bound CoA or acyl-CoA. These structures reveal both hydrophobic and the previously unreported ionic interactions between two-fold-related trimers that build up the cubic core. The entrance of the dihydrolipoamide-binding site in a 30-A long active-site channel is closed in the apo and acyl-CoA-bound structures. CoA binding to one entrance of the channel promotes a conformational change in the channel, resulting in the opening of the opposite dihydrolipoamide gate. Binding experiments show that the affinity of the E2b core for dihydrolipoamide is markedly increased in the presence of CoA. The result buttresses the model that CoA binding is responsible for the opening of the dihydrolipoamide gate. We suggest that this gating mechanism synchronizes the binding of the two substrates to the active-site channel, which serves as a feed-forward switch to coordinate the E2b-catalyzed acyltransfer reaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_17124494}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17124494 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17124494}}
 ==About this Structure==
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 [[Category: Homo trimer]]
 [[Category: Isobutyryl-coa-bound form]]
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