1APS

THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS

1APS の概要

• エントリーDOI: 10.2210/pdb1aps/pdb
• 分子名称: ACYLPHOSPHATASE (1 entity in total)
• 機能のキーワード: hydrolase(acting on acid anhydrides)
• 由来する生物種: Equus caballus (horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11032.44

構造登録者

Saudek, V.,Pastore, A.,Ramponi, G.,Williams, R.J.P. (登録日: 1991-02-20, 公開日: 1992-07-15, 最終更新日: 2024-05-22)

主引用文献

Pastore, A.,Saudek, V.,Ramponi, G.,Williams, R.J.
Three-dimensional structure of acylphosphatase. Refinement and structure analysis.
J.Mol.Biol., 224:427-440, 1992

PubMed Abstract: We report here the complete determination of the solution structure of acylphosphatase, a small enzyme that catalyses the hydrolysis of organic acylphosphates, as determined by distance geometry methods based on nuclear magnetic resonance information. A non-standard strategy for the distance geometry calculations was used and is described here some detail. The five best structures were then refined by restrained energy minimization and molecular dynamics in order to explore the conformational space consistent with the experimental data. We address the question of whether the solution structure of acylphosphatase follows the general principles of protein structure, i.e. those learned from analysing crystal structures. Static and dynamic features are discussed in detail. An uncommon beta-alpha-beta motif, so far found only in procarboxypeptidase B and in an RNA-binding protein, is present in acylphosphatase.

PubMed: 1313885
DOI: 10.1016/0022-2836(92)91005-A

実験手法

SOLUTION NMR