1DP2
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE
Summary for 1DP2
| Entry DOI | 10.2210/pdb1dp2/pdb |
| Related | 1BOH 1BOI 1ORB 1RHD 1RHS 2ORA |
| Descriptor | RHODANESE, 5-[(3S)-1,2-dithiolan-3-yl]pentanoic acid (3 entities in total) |
| Functional Keywords | rhodanese, liopate, sulfurtransferase, transferase |
| Biological source | Bos taurus (cattle) |
| Cellular location | Mitochondrion matrix: P00586 |
| Total number of polymer chains | 1 |
| Total formula weight | 33189.68 |
| Authors | Zanotti, G.,Cianci, M. (deposition date: 1999-12-23, release date: 2000-12-13, Last modification date: 2024-11-06) |
| Primary citation | Cianci, M.,Gliubich, F.,Zanotti, G.,Berni, R. Specific interaction of lipoate at the active site of rhodanese. Biochim.Biophys.Acta, 1481:103-108, 2000 Cited by PubMed Abstract: Dihydrolipoate is an acceptor of the rhodanese-bound sulfane sulfur atom, as shown by analysis of the elementary steps of the reaction catalyzed by rhodanese. The crystal structure of sulfur-substituted rhodanese complexed with the non-reactive oxidized form of lipoate has revealed that the compound is bound at the enzyme active site, with the dithiolane ring buried in the interior of the cavity and the carboxylic end pointing towards the solvent. One of the sulfur atoms of the ligand in the unproductive complex is relatively close to the sulfane sulfur bound to Cys-247, the sulfur that is transferred during the catalytic reaction. This mode of binding of lipoate is likely to mimic that of dihydrolipoate. The results presented here support the possible role of dihydrolipoate as sulfur-acceptor substrate of rhodanese in an enzymatic reaction that might serve to provide iron-sulfur proteins with inorganic sulfide. PubMed: 11004580DOI: 10.1016/S0167-4838(00)00114-X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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