1wnd

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1wnd, resolution 2.10Å

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Escherichia coli YdcW gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal stucture

Overview

In the context of a medium-scaled structural genomics program aiming at, solving the structures of as many as possible bacterial unknown open, reading frame products from Escherichia coli (Y prefix), we have solved, the structure of YdcW at 2.1A resolution, using molecular replacement., According to its sequence identity, YdcW has been classified into the, betaine aldehyde dehydrogenases family (EC 1.2.1.8), catalysing the, oxidation of betaine aldehyde into glycine betaine. The structure of YdcW, resembles that of other aldehyde dehydrogenases: it is tetrameric and, binds a NADH molecule in each monomer. The NADH molecules, bound in the, active site by soaking, are revealed to be in the "hydrolysis position"., Activities experiments demonstrate that YdcW is more active on, medium-chains aldehyde than on betaine aldehyde. However, soaking of, betaine into YdcW crystals revealed its presence in one of the subunits, in two positions, a putative resting position and a hydride transfer ready, position. Analysis of kinetics data and of the active site shape suggest, an optimum binding of n-alkyl aldehydes up to seven to eight carbon atoms, possibly followed by a bulky cyclic or aromatic group.

About this Structure

1WND is a Single protein structure of sequence from Escherichia coli with CA as ligand. Active as Betaine-aldehyde dehydrogenase, with EC number 1.2.1.8 Full crystallographic information is available from OCA.

Reference

Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase., Gruez A, Roig-Zamboni V, Grisel S, Salomoni A, Valencia C, Campanacci V, Tegoni M, Cambillau C, J Mol Biol. 2004 Oct 8;343(1):29-41. PMID:15381418

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