3VRB
Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate
Summary for 3VRB
| Entry DOI | 10.2210/pdb3vrb/pdb |
| Related | 3VR8 |
| Descriptor | Flavoprotein subunit of complex II, PROTOPORPHYRIN IX CONTAINING FE, N-[3-(1-methylethoxy)phenyl]-2-(trifluoromethyl)benzamide, ... (12 entities in total) |
| Functional Keywords | ascaris suum, membrane protein, reductase, mitochondrial membrane, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor |
| Biological source | Ascaris suum (Pig roundworm) More |
| Cellular location | Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side : Q33862 O44074 Mitochondrion inner membrane ; Multi-pass membrane protein : P92507 |
| Total number of polymer chains | 8 |
| Total formula weight | 289071.41 |
| Authors | Shimizu, H.,Shiba, T.,Inaoka, D.K.,Osanai, A.,Kita, K.,Sakamoto, K.,Harada, S. (deposition date: 2012-04-07, release date: 2012-07-11, Last modification date: 2024-11-06) |
| Primary citation | Shimizu, H.,Osanai, A.,Sakamoto, K.,Inaoka, D.K.,Shiba, T.,Harada, S.,Kita, K. Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum J.Biochem., 151:589-592, 2012 Cited by PubMed Abstract: In the anaerobic respiratory chain of the parasitic nematode Ascaris suum, complex II couples the reduction of fumarate to the oxidation of rhodoquinol, a reverse reaction catalyzed by mammalian complex II. In this study, the first structure of anaerobic complex II of mitochondria was determined. The structure, composed of four subunits and five co-factors, is similar to that of aerobic complex II, except for an extra peptide found in the smallest anchor subunit of the A. suum enzyme. We discuss herein the structure-function relationship of the enzyme and the critical role of the low redox potential of rhodoquinol in the fumarate reduction of A. suum complex II. PubMed: 22577165DOI: 10.1093/jb/mvs051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.91 Å) |
Structure validation
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