Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function

被引:19
作者
Davies, C [1 ]
Muirhead, H
机构
[1] Med Univ S Carolina, Dept Biochem & Mol Biol, Charleston, SC 29425 USA
[2] Univ Bristol, Sch Med Sci, Dept Biochem, Bristol BS8 1TD, Avon, England
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷
关键词
D O I
10.1107/S0907444902023387
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Phosphoglucose isomerase (PGI) is a housekeeping enzyme of metabolism that catalyses the interconversion of glucose 6-phosphate and fructose 6-phosphate, with roles in the glycolytic and gluconeogenic pathways. PGI is also a multifunctional protein that manifests the properties of a cytokine in a wide array of cellular processes, including the production of immunoglobulin by B cells and tumour-cell differentiation. The crystal structure of PGI in the native form from rabbit muscle has been solved at a resolution of 2.5 Angstrom by a combination of multiple isomorphous replacement and multicrystal averaging techniques. Comparison with published structures of rabbit PGI in complex with three inhibitors and with the substrate fructose 6-phosphate reveals a number of conformational changes that may be associated with catalytic function. These occur in the small domain around the sugar phosphate-binding site, in a small helix carrying His388 and in a helix near the C-terminal end. One of these may be the structural rearrangement that has been postulated to be the rate-limiting step for catalysis.
引用
收藏
页码:453 / 465
页数:13
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