1KP0

The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus

1KP0 の概要

• エントリーDOI: 10.2210/pdb1kp0/pdb
• 分子名称: CREATINE AMIDINOHYDROLASE (2 entities in total)
• 機能のキーワード: alpha betal, 3-layer(aba) sandwich, hydrolase
• 由来する生物種: Actinobacillus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89452.68

構造登録者

Padmanabhan, B.,Paehler, A.,Horikoshi, M. (登録日: 2001-12-26, 公開日: 2002-07-31, 最終更新日: 2024-10-09)

主引用文献

Padmanabhan, B.,Paehler, A.,Horikoshi, M.
Structure of creatine amidinohydrolase from Actinobacillus.
Acta Crystallogr.,Sect.D, 58:1322-1328, 2002

PubMed Abstract: The crystal structure of Actinobacillus creatine amidinohydrolase has been solved by molecular replacement. The amino-acid sequence has been derived from the crystal structure. Crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4), c = 191.65 (2) A, and contain two molecules in an asymmetric unit. The structure was refined to an R factor of 18.8% at 2.7 A resolution. The crystal structure contains a dimer of 402 residues and 118 water molecules. The protein structure is bilobal, consisting of a small N-terminal domain and a large C-terminal domain. The C-terminal domain has a pitta-bread fold, similar to that found in Pseudomonas putida creatinase, proline aminopeptidases and methionine aminopeptidase. Comparison with complex crystal structures of P. putida creatinase reveals that the enzyme activity of Actinobacillus creatinase might be similar to that of P. putida creatinase.

PubMed: 12136144
DOI: 10.1107/S0907444902010156

実験手法

X-RAY DIFFRACTION (2.7 Å)