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
收藏
页码：1177 / 1181
页数：5
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