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1v16

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[[Category: thiamine diphosphate ]]
[[Category: thiamine diphosphate ]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:37:12 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:18:08 2007''

Revision as of 14:13, 30 October 2007

Image:1v16.gif

1v16, resolution 1.90Å

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CROSSTALK BETWEEN COFACTOR BINDING AND THE PHOSPHORYLATION LOOP CONFORMATION IN THE BCKD MACHINE

Overview

The decarboxylase/dehydrogenase (E1b) component of the 4-megadalton human, branched-chain alpha-keto acid dehydrogenase (BCKD) metabolic machine is a, thiamin diphosphate (ThDP)-dependent enzyme with a heterotetrameric, cofactor-binding fold. The E1b component catalyzes the decarboxylation of, alpha-keto acids and the subsequent reductive acylation of the lipoic, acid-bearing domain (LBD) from the 24-meric transacylase (E2b) core. In, the present study, we show that the binding of cofactor ThDP to the E1b, active site induces a disorder-to-order transition of the conserved, phosphorylation loop carrying the two phosphorylation sites Ser(292)-alpha, and Ser(302)-alpha, as deduced from the 1.80-1.85 A apoE1b and holoE1b, structures. The induced loop conformation is essential for the ... [(full description)]

About this Structure

1V16 is a [Protein complex] structure of sequences from [Homo sapiens] with K, MN, CL, TDP, BEN and GOL as [ligands]. Active as [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [1.2.4.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase., Li J, Wynn RM, Machius M, Chuang JL, Karthikeyan S, Tomchick DR, Chuang DT, J Biol Chem. 2004 Jul 30;279(31):32968-78. Epub 2004 May 27. PMID:15166214

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