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2a1t

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2a1t, resolution 2.80Å ()
Ligands: ,
Activity: Acyl-CoA dehydrogenase, with EC number 1.3.99.3
Domains: MCAD, CaiA, ETF_beta, ETF_alpha, ETF_alpha, FixB
Related: 1t9g, 2a1u
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of the human MCAD:ETF E165betaA complex

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2A1T is a 6 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Toogood HS, van Thiel A, Scrutton NS, Leys D. Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein. J Biol Chem. 2005 Aug 26;280(34):30361-6. Epub 2005 Jun 23. PMID:15975918 doi:10.1074/jbc.M505562200

Page seeded by OCA on Tue Feb 17 21:49:04 2009

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