CRYSTALLIZATION AND OLIGOMERIC STRUCTURE OF RAT-LIVER ARGINASE

被引：40

作者：

KANYO, ZF

CHEN, CY

DAGHIGH, F

ASH, DE

CHRISTIANSON, DW

机构：

[1] UNIV PENN,DEPT CHEM,PHILADELPHIA,PA 19104

[2] TEMPLE UNIV,HLTH SCI CTR,SCH MED,DEPT BIOCHEM,PHILADELPHIA,PA 19140

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 224卷 / 04期

关键词：

ARGINASE; X-RAY CRYSTALLOGRAPHY; METALLOENZYME; PROTEIN STRUCTURE;

D O I：

10.1016/0022-2836(92)90479-4

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：

Rat liver arginase, a manganese-metalloenzyme, has been crystallized from polyethylene glycol 8000 in N,N-bis(2-hydroxyethyl)glycine (Bicine) buffer at pH 8.5. Crystals form as either cubes or pyramids and belong to space group P31 (or P32) with hexagonal unit cell dimensions a = b = 88·9 A ̊, c = 114·8 A ̊, or a = b = 88·5 A ̊, c = 104·5 A ̊; the variation along the c axis does not correlate with the external crystal morphology of cube or pyramidshaped. X-ray diffraction data are measured to a limiting resolution of 2·4 Å. Given the volume constraints of the unit cell it is likely that rat liver arginase is a trimer, with three 35,000 Da monomers in the asymmetric unit. This resolves a persistent ambiguity regarding the oligomeric structure of this enzyme. © 1992.

引用

页码：1175 / 1177

页数：3

共 29 条

[1] THE ACTIVATION OF JACK-BEAN ARGINASE BY COBALT, MANGANESE, AND IRON [J].