2TLD

CRYSTAL STRUCTURE OF AN ENGINEERED SUBTILISIN INHIBITOR COMPLEXED WITH BOVINE TRYPSIN

2TLD の概要

• エントリーDOI: 10.2210/pdb2tld/pdb
• 関連するPDBエントリー: 2SIC 3SIC
• 分子名称: TRYPSIN, STREPTOMYCES SUBTILISIN INHIBITOR (SSI) (2 entities in total)
• 機能のキーワード: proteinase, hydrolase-hydrolase inhibitor complex, trypsin), hydrolase/hydrolase inhibitor
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted, extracellular space: P00760; Secreted: P01006
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34039.29

構造登録者

Mitsui, Y.,Takeuchi, Y.,Nonaka, T.,Nakamura, K.T. (登録日: 1991-09-16, 公開日: 1992-07-15, 最終更新日: 2024-02-21)

主引用文献

Takeuchi, Y.,Nonaka, T.,Nakamura, K.T.,Kojima, S.,Miura, K.,Mitsui, Y.
Crystal structure of an engineered subtilisin inhibitor complexed with bovine trypsin.
Proc.Natl.Acad.Sci.USA, 89:4407-4411, 1992

PubMed Abstract: Proteinase specificity of a proteinaceous inhibitor of subtilisin (SSI; Streptomyces subtilisin inhibitor) can be altered so as to strongly inhibit trypsin simply by replacing P1 methionine with lysine (with or without concomitant change of the P4 residue) through site-directed mutagenesis. Now the crystal structure of one such engineered SSI (P1 methionine converted to lysine and P4 methionine converted to glycine) complexed with bovine trypsin has been solved at 2.6 A resolution and refined to a crystallographic R factor of 0.173. Comparing this structure with the previously established structure of the native SSI complexed with subtilisin BPN', it was found that (i) P1 lysine of the mutant SSI is accommodated in the S1 pocket of trypsin as usual, and (ii) upon complex formation, considerable conformation change occurs to the reactive site loop of the mutant SSI. Thus, in this case, flexibility of the reactive site loop seems important for successfully changing the proteinase specificity through mere replacement of the P1 residue.

PubMed: 1584773
DOI: 10.1073/pnas.89.10.4407

実験手法

X-RAY DIFFRACTION (2.6 Å)