3KZC

Crystal structure of N-acetyl-L-ornithine transcarbamylase

「1YH0」から置き換えられました

3KZC の概要

• エントリーDOI: 10.2210/pdb3kzc/pdb
• 関連するPDBエントリー: 2FG7 3KZK 3KZM 3KZN 3KZO 3L02 3L04 3L05 3L06
• 分子名称: N-acetylornithine carbamoyltransferase, SULFATE ION (3 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 : Q8P8J2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40325.70

構造登録者

Shi, D.,Yu, X.,Allewell, N.M.,Tuchman, M. (登録日: 2009-12-08, 公開日: 2010-03-31, 最終更新日: 2023-11-22)

主引用文献

Shi, D.,Morizono, H.,Yu, X.,Roth, L.,Caldovic, L.,Allewell, N.M.,Malamy, M.H.,Tuchman, M.
Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria.
J.Biol.Chem., 280:14366-14369, 2005

PubMed Abstract: We have identified in Xanthomonas campestris a novel N-acetylornithine transcarbamylase that replaces ornithine transcarbamylase in the canonic arginine biosynthetic pathway of several Eubacteria. The crystal structures of the protein in the presence and absence of the reaction product, N-acetylcitrulline, were determined. This new family of transcarbamylases lacks the DxxSMG motif that is characteristic of all ornithine transcarbamylases (OTCases) and contains a novel proline-rich loop that forms part of the active site. The specificity for N-acetylornithine is conferred by hydrogen bonding with residues in the proline-rich loop via water molecules and by hydrophobic interactions with residues from the adjacent 80's, 120's, and proline-rich loops. This novel protein structure provides a starting point for rational design of specific analogs that may be useful in combating human and plant pathogens that utilize acetylornithine transcarbamylase rather than ornithine transcarbamylase.

PubMed: 15731101
DOI: 10.1074/jbc.C500005200

実験手法

X-RAY DIFFRACTION (2.2 Å)