7KZ5

Crystal structure of KabA from Bacillus cereus UW85 in complex with the plp external aldimine adduct with kanosamine-6-phosphate

7KZ5 の概要

• エントリーDOI: 10.2210/pdb7kz5/pdb
• 関連するPDBエントリー: 7KZ3
• 分子名称: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme, 3-deoxy-3-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-6-O-phosphono-alpha-D-gluco pyranose, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: kanosamine, biosynthesis, aminotransferase, kaba, biosynthetic protein, transferase
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 209100.20

構造登録者

Prasertanan, T.,Palmer, D.R.J.,Sanders, D.A.R. (登録日: 2020-12-10, 公開日: 2021-05-26, 最終更新日: 2023-10-18)

主引用文献

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

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: 33984505
DOI: 10.1016/j.jsb.2021.107744

実験手法

X-RAY DIFFRACTION (1.6 Å)