1TM4

crystal structure of the complex of subtilsin BPN'with chymotrypsin inhibitor 2 M59G mutant

1TM4 の概要

• エントリーDOI: 10.2210/pdb1tm4/pdb
• 関連するPDBエントリー: 1tm1 1tm3 1tm5 1tm7 1TMG 1tO1 1TO2
• 分子名称: Subtilisin BPN' precursor, chymotrypsin inhibitor 2, CALCIUM ION, ... (7 entities in total)
• 機能のキーワード: serine protease, inhibitor, hydrolase
• 由来する生物種: Bacillus amyloliquefaciens; 詳細
• 細胞内の位置: Secreted: P00782
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36753.00

構造登録者

Radisky, E.S.,Kwan, G.,Karen Lu, C.J.,Koshland Jr., D.E. (登録日: 2004-06-10, 公開日: 2004-11-09, 最終更新日: 2023-08-23)

主引用文献

Radisky, E.S.,Kwan, G.,Karen Lu, C.J.,Koshland Jr., D.E.
Binding, Proteolytic, and Crystallographic Analyses of Mutations at the Protease-Inhibitor Interface of the Subtilisin BPN'/Chymotrypsin Inhibitor 2 Complex(,).
Biochemistry, 43:13648-13656, 2004

PubMed Abstract: A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues that interact with the inhibited enzyme subtilisin BPN', were studied to determine the relative importance of intermolecular contacts on either side of the scissile bond. Mutants were tested for inhibition of subtilisin, rates of hydrolysis by subtilisin, and ability to acylate subtilisin. Additionally, crystal structures of the mutant CI2 complexes with subtilisin were obtained. Ordered water molecules were found to play an important role in inhibitor recognition, and features of the crystal structures, in combination with biochemical data, support a transition-state stabilization role for the P(1) residue in subtilisin catalysis. Consistent with the proposed mechanism of inhibition, in which rapid acylation is followed by religation, leaving-group contacts with the enzyme were found to be more critical determinants of inhibition than acylating-group contacts in the mutants studied here.

PubMed: 15504027
DOI: 10.1021/bi048797k

実験手法

X-RAY DIFFRACTION (1.7 Å)