1v11 | pdb_00001v11

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

File:1v11.gif

spinqualitylabelsall models 1v11, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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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