2bs2 | pdb_00002bs2

QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES

spinqualitylabelsall models 2bs2, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bs2 is a 6 chain structure with sequence from Wolinella succinogenes. This structure supersedes the now removed PDB entry 1qla. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: F3S, FAD, FES, FUM, HEM, LMT, NA, SF4 Related: 1e7p, 1qlb, 2bs3, 2bs4 Activity: Succinate dehydrogenase, with EC number 1.3.99.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FRDA_WOLSU] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. [FRDC_WOLSU] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. [FRDB_WOLSU] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Membrane protein complexes can support both the generation and utilisation of a transmembrane electrochemical proton potential ('proton-motive force'), either by transmembrane electron transfer coupled to protolytic reactions on opposite sides of the membrane or by transmembrane proton transfer. Here we provide the first evidence that both of these mechanisms are combined in the case of a specific respiratory membrane protein complex, the dihaem-containing quinol:fumarate reductase (QFR) of Wolinella succinogenes, so as to facilitate transmembrane electron transfer by transmembrane proton transfer. We also demonstrate the non-functionality of this novel transmembrane proton transfer pathway ('E-pathway') in a variant QFR where a key glutamate residue has been replaced. The 'E-pathway', discussed on the basis of the 1.78-Angstrom-resolution crystal structure of QFR, can be concluded to be essential also for the viability of pathogenic varepsilon-proteobacteria such as Helicobacter pylori and is possibly relevant to proton transfer in other dihaem-containing membrane proteins, performing very different physiological functions. Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex.,Madej MG, Nasiri HR, Hilgendorff NS, Schwalbe H, Lancaster CR EMBO J. 2006 Oct 18;25(20):4963-70. Epub 2006 Oct 5. PMID:17024183 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA