1o97
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(New page: 200px<br /> <applet load="1o97" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o97, resolution 1.60Å" /> '''STRUCTURE OF ELECTR...)
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Revision as of 19:21, 29 October 2007
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STRUCTURE OF ELECTRON TRANSFERRING FLAVOPROTEIN FROM METHYLOPHILUS METHYLOTROPHUS, RECOGNITION LOOP REMOVED BY LIMITED PROTEOLYSIS
Overview
Here we report the crystal structures of a ternary electron transfer, complex showing extensive motion at the protein interface. This, physiological complex comprises the iron-sulfur flavoprotein, trimethylamine dehydrogenase and electron transferring flavoprotein (ETF), from Methylophilus methylotrophus. In addition, we report the crystal, structure of free ETF. In the complex, electron density for the FAD domain, of ETF is absent, indicating high mobility. Positions for the FAD domain, are revealed by molecular dynamics simulation, consistent with crystal, structures and kinetic data. A dual interaction of ETF with trimethylamine, dehydrogenase provides for dynamical motion at the protein interface: one, site acts as an anchor, thereby allowing the other site to sample a large, range of ... [(full description)]
About this Structure
1O97 is a [Protein complex] structure of sequences from [Methylophilus methylotrophus] with AMP and FAD as [ligands]. Full crystallographic information is available from [OCA].
Reference
Extensive conformational sampling in a ternary electron transfer complex., Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS, Nat Struct Biol. 2003 Mar;10(3):219-25. PMID:12567183
Page seeded by OCA on Mon Oct 29 21:26:07 2007
