Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila

被引：2

作者：

Siddiqui, Tanzeela ^{[1
,2
]}

Paxman, Jason J. ^{[3
]}

Dogovski, Con ^{[1
,2
]}

Panjikar, Santosh ^{[3
,4
]}

Perugini, Matthew A. ^{[1
,2
]}

机构：

[1] La Trobe Univ, La Trobe Inst Mol Sci, Dept Biochem, Melbourne, Vic 3086, Australia

[2] Univ Melbourne, Dept Biochem & Mol Biol, Mol Sci & Biotechnol Inst Bio21, Melbourne, Vic 3010, Australia

[3] Australian Synchrotron, Melbourne, Vic 3168, Australia

[4] Monash Univ, Dept Biochem & Mol Biol, Melbourne, Vic 3800, Australia

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷

关键词：

AMINO-ACID-REQUIREMENTS; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; MYCOBACTERIUM-TUBERCULOSIS; QUATERNARY STRUCTURE; LYSINE BIOSYNTHESIS; SUSPENSION-CULTURES; BACILLUS-ANTHRACIS; PURIFICATION; EXPRESSION;

D O I：

10.1107/S1744309113024639

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Dihydrodipicolinate synthase (DHDPS) catalyses the rate-limiting step in the biosynthesis of meso-diaminopimelate and lysine. Here, the cloning, expression, purification and crystallization of DHDPS from the intracellular pathogen Legionella pneumophila are described. Crystals grown in the presence of high-molecular-weight PEG precipitant and magnesium chloride were found to diffract beyond 1.65 angstrom resolution. The crystal lattice belonged to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 89.31, c = 290.18 angstrom, and contained two molecules in the asymmetric unit. The crystal structure was determined by molecular replacement using a single chain of Pseudomonas aeruginosa DHDPS as the search model.

引用

页码：1177 / 1181

页数：5

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