2bs3
From Proteopedia
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GLU C180-> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
Overview
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 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].
Reference
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
Page seeded by OCA on Tue Oct 30 12:40:53 2007
Categories: Protein complex | Succinate dehydrogenase | Wolinella succinogenes | Lancaster, C.R.D. | CIT | F3S | FAD | FES | HEM | LMT | NA | SF4 | 2fe-2s | 3d-structure | 3fe-4s | 4fe-4s | Citric acid cycle | Dihaem cytochrome b | Electron transport | Fad | Flavoprotein | Fumarate reductase | Heme | Ion-sulphur protein | Iron | Iron-sulfur | Metal-binding | Oxidoreductase | Respiratory chain | Transmembrane | Tricarboxylic acid cycle