2a1u

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(New page: 200px<br /> <applet load="2a1u" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a1u, resolution 2.11&Aring;" /> '''Crystal structure o...)
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Revision as of 18:38, 12 November 2007

Image:2a1u.gif

2a1u, resolution 2.11Å

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Crystal structure of the human ETF E165betaA mutant

Contents

Overview

Crystal structures of protein complexes with electron-transferring, flavoprotein (ETF) have revealed a dual protein-protein interface with one, region serving as anchor while the ETF FAD domain samples available space, within the complex. We show that mutation of the conserved Glu-165beta in, human ETF leads to drastically modulated rates of interprotein electron, transfer with both medium chain acyl-CoA dehydrogenase and dimethylglycine, dehydrogenase. The crystal structure of free E165betaA ETF is essentially, identical to that of wild-type ETF, but the crystal structure of the, E165betaA ETF.medium chain acyl-CoA dehydrogenase complex reveals clear, electron density for the FAD domain in a position optimal for fast, interprotein electron transfer. Based on our observations, we present a, dynamic multistate model for conformational sampling that for the, wild-type ETF. medium chain acyl-CoA dehydrogenase complex involves random, motion between three distinct positions for the ETF FAD domain. ETF, Glu-165beta plays a key role in stabilizing positions incompatible with, fast interprotein electron transfer, thus ensuring high rates of complex, dissociation.

Disease

Known diseases associated with this structure: Glutaricaciduria, type IIA OMIM:[608053], Glutaricaciduria, type IIB OMIM:[130410]

About this Structure

2A1U is a Protein complex structure of sequences from Homo sapiens with FAD and AMP as ligands. Full crystallographic information is available from OCA.

Reference

Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein., Toogood HS, van Thiel A, Scrutton NS, Leys D, J Biol Chem. 2005 Aug 26;280(34):30361-6. Epub 2005 Jun 23. PMID:15975918

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