1E7P
QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
Summary for 1E7P
| Entry DOI | 10.2210/pdb1e7p/pdb |
| Descriptor | Fumarate reductase flavoprotein subunit, PROTOPORPHYRIN IX CONTAINING FE, DODECYL-BETA-D-MALTOSIDE, ... (11 entities in total) |
| Functional Keywords | oxidoreductase, succinate dehydrogenase, respiratory chain, citric acid cycle, flavoprotein, iron- sulphur protein iron- sulphur protein, dihaem cytochrome b |
| Biological source | Wolinella succinogenes (Vibrio succinogenes) More |
| Total number of polymer chains | 12 |
| Total formula weight | 533040.09 |
| Authors | Lancaster, C.R.D.,Kroeger, A. (deposition date: 2000-09-01, release date: 2001-04-09, Last modification date: 2024-10-23) |
| Primary citation | Lancaster, C.R.D.,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., 268:1820-, 2001 Cited by PubMed Abstract: Quinol:fumarate reductase (QFR) is a membrane protein complex that couples the reduction of fumarate to succinate to the oxidation of quinol to quinone. Previously, the crystal structure of QFR from Wolinella succinogenes was determined based on two different crystal forms, and the site of fumarate binding in the flavoprotein subunit A of the enzyme was located between the FAD-binding domain and the capping domain [Lancaster, C.R.D., Kröger, A., Auer, M., & Michel, H. (1999) Nature 402, 377--385]. Here we describe the structure of W. succinogenes QFR based on a third crystal form and refined at 3.1 A resolution. Compared with the previous crystal forms, the capping domain is rotated in this structure by approximately 14 degrees relative to the FAD-binding domain. As a consequence, the topology of the dicarboxylate binding site is much more similar to those of membrane-bound and soluble fumarate reductase enzymes from other organisms than to that found in the previous crystal forms of W. succinogenes QFR. This and the effects of the replacement of Arg A301 by Glu or Lys by site-directed mutagenesis strongly support a common mechanism for fumarate reduction in this superfamily of enzymes. PubMed: 11248702DOI: 10.1046/J.1432-1327.2001.02053.X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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