1e39
From Proteopedia
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FLAVOCYTOCHROME C3 FROM SHEWANELLA FRIGIDIMARINA HISTIDINE 365 MUTATED TO ALANINE
Overview
The active sites of respiratory fumarate reductases are highly conserved, indicating a common mechanism of action involving hydride and proton, transfer. Evidence from the X-ray structures of substrate-bound fumarate, reductases, including that for the enzyme from Shewanella frigidimarina, [Taylor, P., Pealing, S. L., Reid, G. A., Chapman, S. K., and Walkinshaw, M. D. (1999) Nat. Struct. Biol. 6, 1108-1112], indicates that the, substrate is well positioned to accept a hydride from N5 of the FAD., However, the identity of the proton donor has been the subject of recent, debate and has been variously proposed to be (using numbering for the S., frigidimarina enzyme) His365, His504, and Arg402. We have used, site-directed mutagenesis to examine the roles of these residues in the S., ... [(full description)]
About this Structure
1E39 is a [Single protein] structure of sequence from [Shewanella frigidimarina] with NA, HEC, FAD, FUM and GOL as [ligands]. Full crystallographic information is available from [OCA].
Reference
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study., Doherty MK, Pealing SL, Miles CS, Moysey R, Taylor P, Walkinshaw MD, Reid GA, Chapman SK, Biochemistry. 2000 Sep 5;39(35):10695-701. PMID:10978153
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