1BH6

SUBTILISIN DY IN COMPLEX WITH THE SYNTHETIC INHIBITOR N-BENZYLOXYCARBONYL-ALA-PRO-PHE-CHLOROMETHYL KETONE

1BH6 の概要

• エントリーDOI: 10.2210/pdb1bh6/pdb
• 分子名称: SUBTILISIN DY, CALCIUM ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, subtilisin, protein degradation
• 由来する生物種: Bacillus licheniformis
• 細胞内の位置: Secreted: P00781
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28030.04

構造登録者

Eschenburg, S.,Genov, N.,Wilson, K.S.,Betzel, C. (登録日: 1998-06-15, 公開日: 1998-11-04, 最終更新日: 2024-11-20)

主引用文献

Eschenburg, S.,Genov, N.,Peters, K.,Fittkau, S.,Stoeva, S.,Wilson, K.S.,Betzel, C.
Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg.
Eur.J.Biochem., 257:309-318, 1998

PubMed Abstract: The crystal structure of subtilisin DY inhibited by N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone has been solved by molecular replacement with subtilisin Carlsberg as the starting model. The model has been refined to a crystallographic R factor (= sigma absolute value [(absolute value Fo) - (absolute value Fc)] / sigma (absolute value of Fo) of 15.1% using X-ray diffraction data to 0.175 nm resolution. Subtilisin DY is an alkaline proteinase from the X-irradiated Japanese strain DY of Bacillus licheniformis, which normally produces subtilisin Carlsberg. It has very similar properties to subtilisin Carlsberg, with a slightly enhanced resistance to heat and guanidine hydrochloride-induced denaturation, in spite of the fact that the sequences of the two enzymes differ in 31 positions out of 274 residues. The close similarity in overall three-dimensional structure of subtilisins DY and Carlsberg and also their physicochemical properties, such as activity and stability, shows that nature aided by X-irradiation for rapid 'evolution' is able to accommodate considerable changes in sequence without substantial changes in property.

PubMed: 9826175
DOI: 10.1046/j.1432-1327.1998.2570309.x

実験手法

X-RAY DIFFRACTION (1.75 Å)