1ZUD
Structure of ThiS-ThiF protein complex
Summary for 1ZUD
| Entry DOI | 10.2210/pdb1zud/pdb |
| Descriptor | Adenylyltransferase thiF, ThiS protein, ZINC ION, ... (6 entities in total) |
| Functional Keywords | thiamin, thiazole, protein-protein complex, this, thif, transferase-biosynthetic protein complex, transferase/biosynthetic protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 68870.85 |
| Authors | Ealick, S.E.,Lehmann, C. (deposition date: 2005-05-30, release date: 2006-01-31, Last modification date: 2023-08-23) |
| Primary citation | Lehmann, C.,Begley, T.P.,Ealick, S.E. Structure of the Escherichia coli ThiS-ThiF Complex, a Key Component of the Sulfur Transfer System in Thiamin Biosynthesis. Biochemistry, 45:11-19, 2006 Cited by PubMed Abstract: We have determined the crystal structure of the Escherichia coli ThiS-ThiF protein complex at 2.0 A resolution. ThiS and ThiF are bacterial proteins involved in the synthesis of the thiazole moiety of thiamin. ThiF catalyzes the adenylation of the carboxy terminus of ThiS and the subsequent displacement of AMP catalyzed by ThiI-persulfide to give a ThiS-ThiI acyl disulfide. Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur donor for thiazole formation. ThiS is a small 7.2 kDa protein that structurally resembles ubiquitin and the molybdopterin biosynthetic protein MoaD. ThiF is a 27 kDa protein with distinct sequence and structural similarity to the ubiquitin activating enzyme E1 and the molybdopterin biosynthetic protein MoeB. The ThiF-ThiS structure clarifies the mechanism of the sulfur transfer chemistry involved in thiazole biosynthesis. PubMed: 16388576DOI: 10.1021/bi051502y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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