Summary for 4KEP
| Entry DOI | 10.2210/pdb4kep/pdb |
| Related | 3AJ3 4KEQ |
| Descriptor | 4-pyridoxolactonase, ZINC ION, ACETATE ION, ... (7 entities in total) |
| Functional Keywords | alpha-beta/beta-alpha fold, hydrolase, lactone |
| Biological source | Mesorhizobium loti |
| Total number of polymer chains | 1 |
| Total formula weight | 31291.32 |
| Authors | Kobayashi, J.,Yoshikane, Y.,Baba, S.,Mizutani, K.,Takahashi, N.,Mikami, B.,Yagi, T. (deposition date: 2013-04-26, release date: 2014-04-09, Last modification date: 2023-11-08) |
| Primary citation | Kobayashi, J.,Yoshikane, Y.,Yagi, T.,Baba, S.,Mizutani, K.,Takahashi, N.,Mikami, B. Structure of 4-pyridoxolactonase from Mesorhizobium loti. Acta Crystallogr.,Sect.F, 70:424-432, 2014 Cited by PubMed Abstract: 4-Pyridoxolactonase from Mesorhizobium loti catalyzes the zinc-dependent lactone-ring hydrolysis of 4-pyridoxolactone (4PAL) to 4-pyridoxic acid (4PA) in vitamin B6 degradation pathway I. The crystal structures of 4-pyridoxolactonase and its complex with 5-pyridoxolactone (5PAL; the competitive inhibitor) were determined. The overall structure was an αβ/βα sandwich fold, and two zinc ions were coordinated. This strongly suggested that the enzyme belongs to subclass B3 of the class B β-lactamases. In the complex structure, the carbonyl group of 5PAL pointed away from the active site, revealing why it acts as a competitive inhibitor. Based on docking simulation with 4PAL, 4PA and a reaction intermediate, 4-pyridoxolactonase probably catalyzes the reaction through a subclass B2-like mechanism, not the subclass B3 mechanism. PubMed: 24699732DOI: 10.1107/S2053230X14003926 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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