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2bs2
From Proteopedia
| 2bs2, resolution 1.78Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , , , , , and | ||||||||
| Ligands: | , , , , , , , | ||||||||
| Activity: | Succinate dehydrogenase, with EC number 1.3.99.1 | ||||||||
| Related: | 1e7p, 1qlb, 2bs3, 2bs4 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
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.
About this Structure
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.
Reference
- Madej MG, Nasiri HR, Hilgendorff NS, Schwalbe H, Lancaster CR. Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex. EMBO J. 2006 Oct 18;25(20):4963-70. Epub 2006 Oct 5. PMID:17024183
- Lancaster CR. Wolinella succinogenes quinol:fumarate reductase-2.2-A resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer. Biochim Biophys Acta. 2002 Oct 11;1565(2):215-31. PMID:12409197
- Lancaster CR, Gross R, Simon J. A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction. Eur J Biochem. 2001 Mar;268(6):1820-7. PMID:11248702
- Lancaster CR, Gorss R, Haas A, Ritter M, Mantele W, Simon J, Kroger A. Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes fumarate reductase. Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13051-6. PMID:11186225
- Lancaster CR, Kroger A, Auer M, Michel H. Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution. Nature. 1999 Nov 25;402(6760):377-85. PMID:10586875 doi:10.1038/46483
Categories: Succinate dehydrogenase | Wolinella succinogenes | Lancaster, C R.D. | 2fe-2 | 3fe-4 | 4fe-4 | 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

