3QH2
Crystal structure of TenI from Bacillus subtilis complexed with product cThz-P
Summary for 3QH2
| Entry DOI | 10.2210/pdb3qh2/pdb |
| Descriptor | Regulatory protein tenI, 4-methyl-5-[2-(phosphonooxy)ethyl]-1,3-thiazole-2-carboxylic acid, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | alpha-beta barrel, isomerase |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 4 |
| Total formula weight | 100267.00 |
| Authors | Han, Y.,Zhang, Y.,Hazra, A.,Chatterjee, A.,Lai, R.,Begley, T.P.,Ealick, S.E. (deposition date: 2011-01-25, release date: 2011-05-25, Last modification date: 2023-09-13) |
| Primary citation | Hazra, A.B.,Han, Y.,Chatterjee, A.,Zhang, Y.,Lai, R.Y.,Ealick, S.E.,Begley, T.P. A Missing Enzyme in Thiamin Thiazole Biosynthesis: Identification of TenI as a Thiazole Tautomerase. J.Am.Chem.Soc., 133:9311-9319, 2011 Cited by PubMed Abstract: In many bacteria tenI is found clustered with genes involved in thiamin thiazole biosynthesis. However, while TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity, and the role of this enzyme in thiamin biosynthesis remains unknown. In this contribution, we identify the function of TenI as a thiazole tautomerase, describe the structure of the enzyme complexed with its reaction product, identify the substrates phosphate and histidine 122 as the acid/base residues involved in catalysis, and propose a mechanism for the reaction. The identification of the function of TenI completes the identification of all of the enzymes needed for thiamin biosynthesis by the major bacterial pathway. PubMed: 21534620DOI: 10.1021/ja1110514 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.231 Å) |
Structure validation
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