CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC CHARACTERIZATION OF ASPARTIC PROTEINASE-A FROM BAKERS-YEAST AND ITS COMPLEXES WITH INHIBITORS

被引：4

作者：

BADASSO, M

WOOD, SP

AGUILAR, C

COOPER, JB

BLUNDELL, TL

DREYER, T

机构：

[1] UNIV LONDON BIRKBECK COLL,MOLEC BIOL LAB,LONDON WC1E 7HX,ENGLAND

[2] UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,IMPERIAL CANC RES FUND,STRUCT MOLEC BIOL UNIT,LONDON WC1E 7HX,ENGLAND

[3] CARLSBERG LAB,DEPT CHEM,DK-2500 COPENHAGEN,DENMARK

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 232卷 / 02期

关键词：

ASPARTIC PROTEINASES; SACCHAROMYCES-CEREVISIAE; PROTEINASE-A; CRYSTALLIZATION; X-RAY ANALYSIS;

D O I：

10.1006/jmbi.1993.1420

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 aspartic proteinase from yeast vacuoles, proteinase-A, has been crystallized with and without non-hydrolysable transition-state analogue inhibitors. The native enzyme crystals belong to the space group I212121, with two molecules per asymmetric unit. The inhibitor complex crystals are trigonal with space group P3221 and with one molecule in the asymmetric unit. Preliminary X-ray analysis of both native enzyme and its complexes indicate that the complexes diffract to higher resolution than the native crystals. This is probably due to reduced flexibility in the enzyme-inhibitor complex.

引用

页码：701 / 703

页数：3

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