1qo8

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1qo8, resolution 2.15Å

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THE STRUCTURE OF THE OPEN CONFORMATION OF A FLAVOCYTOCHROME C3 FUMARATE REDUCTASE

Overview

Fumarate reductases and succinate dehydrogenases play central roles in the, metabolism of eukaryotic and prokaryotic cells. A recent medium resolution, structure of the Escherichia coli fumarate reductase (Frd) has revealed, the overall organization of the membrane-bound complex. Here we present, the first high resolution X-ray crystal structure of a water-soluble, bacterial fumarate reductase in an open conformation. This structure, reveals a mobile domain that modulates substrate access to the active site, and provides new insights into the mechanism of this widespread and, important family of FAD-containing respiratory proteins.

About this Structure

1QO8 is a Single protein structure of sequence from Shewanella frigidimarina with HEM and FAD as ligands. Active as Succinate dehydrogenase, with EC number 1.3.99.1 Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9 and BC1. Full crystallographic information is available from OCA.

Reference

Open conformation of a flavocytochrome c3 fumarate reductase., Bamford V, Dobbin PS, Richardson DJ, Hemmings AM, Nat Struct Biol. 1999 Dec;6(12):1104-7. PMID:10581549

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