4K2B
Crystal structure of ntda from bacillus subtilis in complex with the internal aldimine
4K2B の概要
| エントリーDOI | 10.2210/pdb4k2b/pdb |
| 関連するPDBエントリー | 4K2I 4K2M |
| 分子名称 | NTD biosynthesis operon protein NtdA (2 entities in total) |
| 機能のキーワード | sugar aminotransferase, aspertate aminotransferase fold, homo-dimer, additional n-terninal domain, transferase |
| 由来する生物種 | Bacillus subtilis subsp. subtilis |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 100865.27 |
| 構造登録者 | Van Straaten, K.E.,Palmer, D.R.J.,Sanders, D.A.R. (登録日: 2013-04-08, 公開日: 2013-10-16, 最終更新日: 2024-03-13) |
| 主引用文献 | van Straaten, K.E.,Ko, J.B.,Jagdhane, R.,Anjum, S.,Palmer, D.R.,Sanders, D.A. The Structure of NtdA, a Sugar Aminotransferase Involved in the Kanosamine Biosynthetic Pathway in Bacillus subtilis, Reveals a New Subclass of Aminotransferases. J.Biol.Chem., 288:34121-34130, 2013 Cited by PubMed Abstract: NtdA from Bacillus subtilis is a sugar aminotransferase that catalyzes the pyridoxal phosphate-dependent equatorial transamination of 3-oxo-α-D-glucose 6-phosphate to form α-D-kanosamine 6-phosphate. The crystal structure of NtdA shows that NtdA shares the common aspartate aminotransferase fold (Type 1) with residues from both monomers forming the active site. The crystal structures of NtdA alone, co-crystallized with the product α-D-kanosamine 6-phosphate, and incubated with the amine donor glutamate reveal three key structures in the mechanistic pathway of NtdA. The structure of NtdA alone reveals the internal aldimine form of NtdA with the cofactor pyridoxal phosphate covalently attached to Lys-247. The addition of glutamate results in formation of pyridoxamine phosphate. Co-crystallization with kanosamine 6-phosphate results in the formation of the external aldimine. Only α-D-kanosamine 6-phosphate is observed in the active site of NtdA, not the β-anomer. A comparison of the structure and sequence of NtdA with other sugar aminotransferases enables us to propose that the VIβ family of aminotransferases should be divided into subfamilies based on the catalytic lysine motif. PubMed: 24097983DOI: 10.1074/jbc.M113.500637 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.31 Å) |
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