2bs3

File:2bs3.gif

spinqualitylabelsall models 2bs3, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

GLU C180-> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES

OverviewOverview

Reconciliation of apparently contradictory experimental results obtained, on the quinol:fumarate reductase, a diheme-containing respiratory membrane, protein complex from Wolinella succinogenes, was previously obtained by, the proposal of the so-called "E pathway hypothesis." According to this, hypothesis, transmembrane electron transfer via the heme groups is, strictly coupled to cotransfer of protons via a transiently established, pathway thought to contain the side chain of residue Glu-C180 as the most, prominent component. Here we demonstrate that, after replacement of, Glu-C180 with Gln or Ile by site-directed mutagenesis, the resulting, mutants are unable to grow on fumarate, and the membrane-bound variant, enzymes lack quinol oxidation activity. Upon solubilization, however, the, ... [(full description)]

About this StructureAbout this Structure

2BS3 is a [Protein complex] structure of sequences from [Wolinella succinogenes] with NA, FAD, CIT, FES, F3S, SF4, HEM and LMT as [ligands]. Active as [Succinate dehydrogenase], with EC number [1.3.99.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase., Lancaster CR, Sauer US, Gross R, Haas AH, Graf J, Schwalbe H, Mantele W, Simon J, Madej MG, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18860-5. PMID:16380425

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