7KZ3
Crystal structure of KabA from Bacillus cereus UW85 in complex with the internal aldimine
Summary for 7KZ3
| Entry DOI | 10.2210/pdb7kz3/pdb |
| Descriptor | Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme, 1,2-ETHANEDIOL, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | kanosamine, biosynthesis, aminotransferase, kaba, biosynthetic protein, transferase |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 4 |
| Total formula weight | 209176.78 |
| Authors | Prasertanan, T.,Palmer, D.R.J.,Sanders, D.A.R. (deposition date: 2020-12-09, release date: 2021-05-26, Last modification date: 2023-11-15) |
| Primary citation | Prasertanan, T.,Palmer, D.R.J.,Sanders, D.A.R. Snapshots along the catalytic path of KabA, a PLP-dependent aminotransferase required for kanosamine biosynthesis in Bacillus cereus UW85. J.Struct.Biol., 213:107744-107744, 2021 Cited by PubMed Abstract: Kanosamine is an antibiotic and antifungal monosaccharide. The kanosamine biosynthetic pathway from glucose 6-phosphate in Bacillus cereus UW85 was recently reported, and the functions of each of the three enzymes in the pathway, KabA, KabB and KabC, were demonstrated. KabA, a member of a subclass of the VI family of PLP-dependent aminotransferases, catalyzes the second step in the pathway, generating kanosamine 6-phosphate (K6P) using l-glutamate as the amino-donor. KabA catalysis was shown to be extremely efficient, with a second-order rate constant with respect to K6P transamination of over 10 Ms. Here we report the high-resolution structure of KabA in both the PLP- and PMP-bound forms. In addition, co-crystallization with K6P allowed the structure of KabA in complex with the covalent PLP-K6P adduct to be solved. Co-crystallization or soaking with glutamate or 2-oxoglutarate did not result in crystals with either substrate/product. Reduction of the PLP-KabA complex with sodium cyanoborohydride gave an inactivated enzyme, and crystals of the reduced KabA were soaked with the l-glutamate analog glutarate to mimic the KabA-PLP-l-glutamate complex. Together these four structures give a complete picture of how the active site of KabA recognizes substrates for each half-reaction. The KabA structure is discussed in the context of homologous aminotransferases. PubMed: 33984505DOI: 10.1016/j.jsb.2021.107744 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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