2GV1

NMR solution structure of the Acylphosphatase from Eschaerichia Coli

2GV1 の概要

• エントリーDOI: 10.2210/pdb2gv1/pdb
• 関連するPDBエントリー: 1APS 1Y9O 2ACY
• 分子名称: Probable acylphosphatase (1 entity in total)
• 機能のキーワード: globular alpha-helix/beta-sheet protein, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10314.76

構造登録者

Pagano, K.,Corazza, A.,Viglino, P.,Esposito, G. (登録日: 2006-05-02, 公開日: 2006-10-31, 最終更新日: 2024-10-16)

主引用文献

Pagano, K.,Ramazzotti, M.,Viglino, P.,Esposito, G.,Degl'innocenti, D.,Taddei, N.,Corazza, A.
NMR solution structure of the acylphosphatase from Escherichia coli.
J.Biomol.Nmr, 36:199-204, 2006

PubMed Abstract: The solution structure of Escherichia coli acylphosphatase (E. coli AcP), a small enzyme catalyzing the hydrolysis of acylphosphates, was determined by (1)H and (15)N NMR and restrained modelling calculation. In analogy with the other members of AcP family, E. coli AcP shows an alpha/beta sandwich domain composed of four antiparallel and one parallel beta-strand, assembled in a five-stranded beta-sheet facing two antiparallel alpha-helices. The pairwise RMSD values calculated for the backbone atoms of E. coli and Sulfolobus solfataricus AcP, Bovine common type AcP and Horse muscle AcP are 2.18, 5.31 and 5.12 A, respectively. No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures.

PubMed: 17021943
DOI: 10.1007/s10858-006-9073-2

実験手法

SOLUTION NMR