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2beu

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(New page: 200px<br /> <applet load="2beu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2beu, resolution 1.89&Aring;" /> '''REACTIVITY MODULATI...)
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Revision as of 18:52, 29 October 2007

Image:2beu.gif

2beu, resolution 1.89Å

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REACTIVITY MODULATION OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCH

Overview

The dehydrogenase/decarboxylase (E1b) component of the 4 MD human, branched-chain alpha-ketoacid dehydrogenase complex (BCKDC) is a thiamin, diphosphate (ThDP)-dependent enzyme. We have determined the crystal, structures of E1b with ThDP bound intermediates after decarboxylation of, alpha-ketoacids. We show that a key tyrosine residue in the E1b active, site functions as a conformational switch to reduce the reactivity of the, ThDP cofactor through interactions with its thiazolium ring. The, intermediates do not assume the often-postulated enamine state, but likely, a carbanion state. The carbanion presumably facilitates the second, E1b-catalyzed reaction, involving the transfer of an acyl moiety from the, intermediate to a lipoic acid prosthetic group in the transacylase (E2b), component ... [(full description)]

About this Structure

2BEU is a [Protein complex] structure of sequences from [Homo sapiens] with CL, K, MN, SO4, THV and GOL as [ligands]. Active as [[1]], with EC number [1.2.4.4]. Full crystallographic information is available from [OCA].

Reference

A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase., Machius M, Wynn RM, Chuang JL, Li J, Kluger R, Yu D, Tomchick DR, Brautigam CA, Chuang DT, Structure. 2006 Feb;14(2):287-98. PMID:16472748

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