CRYSTAL-STRUCTURE OF AN ALKALINE PROTEASE FROM BACILLUS-ALCALOPHILUS AT 2.4 A RESOLUTION

被引：12

作者：

SOBEK, H ^{[1
]}

HECHT, HJ ^{[1
]}

HOFMANN, B ^{[1
]}

AEHLE, W ^{[1
]}

SCHOMBURG, D ^{[1
]}

机构：

[1] GESELL BIOTECHNOL FORSCH GMBH,MASCHERODER WEG 1,W-3300 BRAUNSCHWEIG,GERMANY

来源：

FEBS LETTERS | 1990年 / 274卷 / 1-2期

关键词：

Alkaline protease; Bacillus alcalophilus; Crystal structure; Crystallization;

D O I：

10.1016/0014-5793(90)81328-L

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of an alkaline protease from Bacillus alcahphilus has been determined by X-ray diffraction at 2.4 Å resolution. The enzyme crystallizes in space group P212121, with lattice constants a = 53.7, b = 61.6, c = 75.9 Å. The structure was solved by molecular replacement using the structure of subtilisin Carlsberg as search model. Refinement using molecular dynamics and restrained least squares methods results in a crystallographic R-factor of 0.185. The tertiary structure is very similar to that of subtilisin Carlsberg. The greatest structural differences occur in loops at the surface of the protein. © 1990.

引用

页码：57 / 60

页数：4

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