Summary for 2BS2
| Entry DOI | 10.2210/pdb2bs2/pdb |
| Related | 1E7P 1QLB 2BS3 2BS4 |
| Descriptor | QUINOL-FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT A, PROTOPORPHYRIN IX CONTAINING FE, DODECYL-BETA-D-MALTOSIDE, ... (12 entities in total) |
| Functional Keywords | oxidoreductase, respiratory chain, citric acid cycle, iron-sulphur protein |
| Biological source | WOLINELLA SUCCINOGENES More |
| Total number of polymer chains | 6 |
| Total formula weight | 268107.79 |
| Authors | Lancaster, C.R.D. (deposition date: 2005-05-14, release date: 2006-10-25, Last modification date: 2024-10-23) |
| Primary citation | Madej, M.G.,Nasiri, H.R.,Hilgendorff, N.S.,Schwalbe, H.,Lancaster, C.R.D. Evidence for Transmembrane Proton Transfer in a Dihaem-Containing Membrane Protein Complex. Embo J., 25:4963-, 2006 Cited by PubMed Abstract: 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 epsilon-proteobacteria such as Helicobacter pylori and is possibly relevant to proton transfer in other dihaem-containing membrane proteins, performing very different physiological functions. PubMed: 17024183DOI: 10.1038/SJ.EMBOJ.7601361 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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