6EHQ

E. coli Hydrogenase-2 (as isolated form).

Summary for 6EHQ

• Entry DOI: 10.2210/pdb6ehq/pdb
• Descriptor: Hydrogenase-2 small chain, Hydrogenase-2 large chain, IRON/SULFUR CLUSTER, ... (8 entities in total)
• Functional Keywords: nife hydrogenase, membrane protein, hydrogen oxidation, oxidoreductase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 4
• Total formula weight: 189763.87

Authors

Carr, S.B.,Beaton, S.E.,Evans, R.M.,Armstrong, F.A. (deposition date: 2017-09-14, release date: 2018-04-18, Last modification date: 2024-11-06)

Primary citation

Beaton, S.E.,Evans, R.M.,Finney, A.J.,Lamont, C.M.,Armstrong, F.A.,Sargent, F.,Carr, S.B.
The structure of hydrogenase-2 fromEscherichia coli: implications for H2-driven proton pumping.
Biochem. J., 475:1353-1370, 2018

PubMed Abstract: Under anaerobic conditions, is able to metabolize molecular hydrogen via the action of several [NiFe]-hydrogenase enzymes. Hydrogenase-2, which is typically present in cells at low levels during anaerobic respiration, is a periplasmic-facing membrane-bound complex that functions as a proton pump to convert energy from hydrogen (H) oxidation into a proton gradient; consequently, its structure is of great interest. Empirically, the complex consists of a tightly bound core catalytic module, comprising large (HybC) and small (HybO) subunits, which is attached to an Fe-S protein (HybA) and an integral membrane protein (HybB). To date, efforts to gain a more detailed picture have been thwarted by low native expression levels of Hydrogenase-2 and the labile interaction between HybOC and HybA/HybB subunits. In the present paper, we describe a new overexpression system that has facilitated the determination of high-resolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex.

PubMed: 29555844
DOI: 10.1042/BCJ20180053

Experimental method

X-RAY DIFFRACTION (2.2 Å)