A structural variation for MurB:: X-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB)

被引：52

作者：

Benson, TE

Harris, MS

Choi, GH

Cialdella, JI

Herberg, JT

Martin, JP

Baldwin, ET

机构：

[1] Pharmacia Corp, Struct Analyt & Med Chem Biol & Prot Sci, Kalamazoo, MI 49007 USA

[2] Human Genome Sci Inc, Mol Biol, Rockville, MD 20850 USA

来源：

BIOCHEMISTRY | 2001年 / 40卷 / 08期

关键词：

D O I：

10.1021/bi002162d

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 X-ray crystal structure of the substrate free form of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB) has been solved to 2.3 Angstrom resolution with an R-factor of 20.3% and a free R-factor of 22.3%. While the overall fold of the S. aureus enzyme is similar to that of the homologous Escherichia coli MurB X-ray crystal structure, notable distinctions between the S. aureus and E. coli MurB protein structures occur in residues involved in substrate binding. Analysis of available MurB sequences from other bacteria suggest that the S. aureus MurB structure is representative of a distinct structural class of UDP-N-acetylenolpyruvylglucosamine reductases including Bacillus subtilis and Helicobacter pylori that are characterized by a modified mechanism for substrate binding.

引用

页码：2340 / 2350

页数：11

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[1] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].