1v11

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spinqualitylabelsall models 1v11, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

1V11 is a [Protein complex] structure of sequences from [Homo sapiens] with K, MN, CL, TDP, BEN and GOL as [ligands]. Active as [[1]], with EC number [1.2.4.4]. 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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