Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from Agrobacterium tumefaciens

被引：7

作者：

Atkinson, Sarah C. ^{[1
,2
]}

Dogovski, Con ^{[1
]}

Dobson, Renwick C. J. ^{[2
,3
]}

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] Univ Canterbury, Biomol Interact Ctr, Sch Biol Sci, Christchurch 1, New Zealand

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2012年 / 68卷

基金：

澳大利亚研究理事会;

关键词：

crown gall disease; herbicides; lysine metabolism; quaternary structure; RAY DIFFRACTION ANALYSIS; ESCHERICHIA-COLI; CROWN-GALL; CRYSTAL-STRUCTURE; LYSINE BIOSYNTHESIS; GRAPE; CRYSTALLOGRAPHY; SPECIFICITY; RESISTANCE; CATALYSIS;

D O I：

10.1107/S1744309112033052

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Dihydrodipicolinate synthase (DHDPS) catalyzes the first committed step of the lysine-biosynthesis pathway in bacteria, plants and some fungi. This study describes the cloning, expression, purification and crystallization of DHDPS (NP_354047.1) from the plant pathogen Agrobacterium tumefaciens (AgT-DHDPS). Enzyme-kinetics studies demonstrate that AgT-DHDPS possesses DHDPS activity in vitro. Crystals of AgT-DHDPS were grown in the unliganded form and in forms with substrate bound and with substrate plus allosteric inhibitor (lysine) bound. X-ray diffraction data sets were subsequently collected to a maximum resolution of 1.40 angstrom. Determination of the structure with and without substrate and inhibitor will offer insight into the design of novel pesticide agents.

引用

页码：1040 / 1047

页数：8

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