3KZO
Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate and N-acetyl-L-norvaline
「1ZQ8」から置き換えられました3KZO の概要
| エントリーDOI | 10.2210/pdb3kzo/pdb |
| 関連するPDBエントリー | 2FG7 3KZC 3KZK 3KZM 3KZN 3L02 3L04 3L05 3L06 |
| 分子名称 | N-acetylornithine carbamoyltransferase, N-ACETYL-L-NORVALINE, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, ... (6 entities in total) |
| 機能のキーワード | transcarbamylase, amino-acid biosynthesis, arginine biosynthesis, cytoplasm, transferase |
| 由来する生物種 | Xanthomonas campestris pv. campestris |
| 細胞内の位置 | Cytoplasm (Probable): Q8P8J2 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 40621.93 |
| 構造登録者 | |
| 主引用文献 | Shi, D.,Yu, X.,Roth, L.,Morizono, H.,Tuchman, M.,Allewell, N.M. Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins, 64:532-542, 2006 Cited by PubMed Abstract: N-acetyl-L-ornithine transcarbamoylase (AOTCase) is a new member of the transcarbamoylase superfamily that is essential for arginine biosynthesis in several eubacteria. We report here crystal structures of the binary complexes of AOTCase with its substrates, carbamoyl phosphate (CP) or N-acetyl-L-ornithine (AORN), and the ternary complex with CP and N-acetyl-L-norvaline. Comparison of these structures demonstrates that the substrate-binding mechanism of this novel transcarbamoylase is different from those of aspartate and ornithine transcarbamoylases, both of which show ordered substrate binding with large domain movements. CP and AORN bind to AOTCase independently, and the main conformational change upon substrate binding is ordering of the 80's loop, with a small domain closure around the active site and little movement of the 240's loop. The structures of the complexes provide insight into the mode of substrate binding and the mechanism of the transcarbamoylation reaction. PubMed: 16741992DOI: 10.1002/prot.21013 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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