The 1.70 Å X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase

被引：11

作者：

Müller, P ^{[1
]}

Sawaya, MR ^{[1
]}

Pashkov, I ^{[1
]}

Chan, S ^{[1
]}

Nguyen, C ^{[1
]}

Wu, Y ^{[1
]}

Perry, LJ ^{[1
]}

Eisenberg, D ^{[1
]}

机构：

[1] Howard Hughes Med Inst, UCLA DOE Inst Genom & Proteom, Los Angeles, CA 90095 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2005年 / 61卷

关键词：

D O I：

10.1107/S0907444904033190

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The single-crystal X-ray structure of phosphoglycerate mutase from Mycobacterium tuberculosis has been determined at a resolution of 1.70 Angstrom. The C-terminal tail of each of the subunits is flexible and disordered; however, for one of the four chains (chain A) all but five residues of the chain could be modeled. Noteworthy features of the structure include the active site and a proline-rich segment in each monomer forming a short left-handed polyprolyl helix. These segments lie on the enzyme surface and could conceivably participate in protein-protein interactions.

引用

页码：309 / 315

页数：7

共 31 条

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