Crystallization and preliminary X-ray diffraction analysis of phosphoglucose isomerase from Pyrococcus furiosus

被引：4

作者：

Swan, MK

Hansen, T

Schönheit, P

Davies, C ^{[1
]}

机构：

[1] Med Univ S Carolina, Dept Biochem & Mol Biol, Charleston, SC 29425 USA

[2] Univ Kiel, Inst Allgemeine Mikrobiol, D-24118 Kiel, Germany

来源：

PROTEIN AND PEPTIDE LETTERS | 2003年 / 10卷 / 05期

关键词：

Pyrococcus furiosus; phosphoglucose isomerase; cupin fold; X-ray crystallography;

D O I：

10.2174/0929866033478762

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：

In several euryarchaeota, phosphoglucose isomerase (PGI) activity is catalyzed by an enzyme unrelated to the well-known family of PGI enzymes found in prokaryotes, eukaryotes and some archaea. In order to understand the mechanistic differences between the two families of enzymes we have crystallized PGI from the archaeon Pyrococcus furiosus. The crystals belong to the space group P2(1) and a complete dataset extending to 1.9 Angstrom resolution has been collected.

引用

页码：517 / 520

页数：4

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