1XVM

Trypsin from Fusarium oxysporum- room temperature to atomic resolution

1XVM の概要

• エントリーDOI: 10.2210/pdb1xvm/pdb
• 関連するPDBエントリー: 1PPZ 1PQ5 1PQ8 1PQA 1XVO
• 分子名称: Trypsin, substrate tripeptide GLY-ALA-ARG (3 entities in total)
• 機能のキーワード: atomic resolution, mobility, room temperature, hydrolase
• 由来する生物種: Fusarium oxysporum; 詳細
• 細胞内の位置: Secreted: P35049
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22503.83

構造登録者

Schmidt, A.,Lamzin, V.S. (登録日: 2004-10-28, 公開日: 2005-07-26, 最終更新日: 2024-10-30)

主引用文献

Schmidt, A.,Lamzin, V.S.
Extraction of functional motion in trypsin crystal structures.
Acta Crystallogr.,Sect.D, 61:1132-1139, 2005

PubMed Abstract: The analysis of anisotropic atomic displacement parameters for the direct extraction of functionally relevant motion from X-ray crystal structures of Fusarium oxysporum trypsin is presented. Several atomic resolution structures complexed with inhibitors or substrates and determined at different pH values and temperatures were investigated. The analysis revealed a breathing-like molecular motion conserved across trypsin structures from two organisms and three different crystal forms. Directional motion was observed suggesting a change of the width of the substrate-binding cleft and a change in the length of the specificity pocket. The differences in direction of motion across the structures are dependent on the mode of substrate or inhibitor binding and the chemical environment around the active-site residues. Together with the occurrence of multiple-residue conformers, they reflect spatial rearrangement throughout the deacylation pathway.

PubMed: 16041079
DOI: 10.1107/S0907444905016732

実験手法

X-RAY DIFFRACTION (1.1 Å)