QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES

File:1e7p.gif


1e7p, resolution 3.10Å

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OverviewOverview

Quinol:fumarate reductase (QFR) is a membrane protein complex that couples, the reduction of fumarate to succinate to the oxidation of quinol to, quinone. Previously, the crystal structure of QFR from Wolinella, succinogenes was determined based on two different crystal forms, and the, site of fumarate binding in the flavoprotein subunit A of the enzyme was, located between the FAD-binding domain and the capping domain [Lancaster, C.R.D., Kroger, A., Auer, M., & Michel, H. (1999) Nature 402, 377--385]., Here we describe the structure of W. succinogenes QFR based on a third, crystal form and refined at 3.1 A resolution. Compared with the previous, crystal forms, the capping domain is rotated in this structure by, approximately 14 degrees relative to the FAD-binding domain. As a, ... [(full description)]

About this StructureAbout this Structure

1E7P is a [Protein complex] structure of sequences from [Wolinella succinogenes] with NA, HEM, FES, F3S, SF4, FAD, MLA and LMT as [ligands]. Active as [Succinate dehydrogenase], with EC number [1.3.99.1]. Structure known Active Sites: FA1, FA2, FA3, FA4, FS1, FS2, FS3, FS4, FS5, FS6, FS7, FS8, FS9, FSA, FSB, FSC, HE1, HE2, HE3 and HE4. Full crystallographic information is available from [OCA].

ReferenceReference

A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction., Lancaster CR, Gross R, Simon J, Eur J Biochem. 2001 Mar;268(6):1820-7. PMID:11248702

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