1bkj

From Proteopedia

Revision as of 12:50, 30 October 2007

NADPH:FMN OXIDOREDUCTASE FROM VIBRIO HARVEYI

Overview

We report the structure of an NADPH:FMN oxidoreductase (flavin reductase, P) that is involved in bioluminescence by providing reduced FMN to, luciferase. The 1.8 A crystal structure of flavin reductase P from Vibrio, harveyi was solved by multiple isomorphous replacement and reveals that, the enzyme is a unique dimer of interlocking subunits, with 9352 A2 of, surface area buried in the dimer interface. Each subunit comprises two, domains. The first domain consists of a four-stranded antiparallel, beta-sheet flanked by helices on either side. The second domain reaches, out from one subunit and embraces the other subunit and is responsible for, interlocking the two subunits. Our structure explains why flavin reductase, P is specific for FMN as cofactor. FMN is recognized and tightly bound ... [(full description)]

About this Structure

1BKJ is a [Single protein] structure of sequence from [Vibrio harveyi] with PO4 and FMN as [ligands]. This structure superseeds the now removed PDB entry 1CUM. Active as [Transferred entry: 1.5.1.29], with EC number [1.6.8.1]. Structure known Active Sites: ASA and ASB. Full crystallographic information is available from [OCA].

Reference

Flavin reductase P: structure of a dimeric enzyme that reduces flavin., Tanner JJ, Lei B, Tu SC, Krause KL, Biochemistry. 1996 Oct 22;35(42):13531-9. PMID:8885832

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