Open AccessCloning, expression, crystallization and preliminary structural studies of dihydrodipicolinate reductase from Acinetobacter baumannii
Author(s) -
Kaushik Sanket,
Singh Avinash,
Sinha Mau,
Kaur Punit,
Sharma Sujata,
Singh Tej P.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113011214
Subject(s) - acinetobacter baumannii , orthorhombic crystal system , bacteria , enzyme , microbiology and biotechnology , reductase , antibiotics , biology , stereochemistry , biochemistry , chemistry , crystallography , crystal structure , genetics , pseudomonas aeruginosa
Acinetobacter baumannii is a virulent pathogenic bacterium that is resistant to most currently available antibiotics. Therefore, the design of drugs for the treatment of infections caused by A. baumannii is urgently required. Dihydrodipicolinate reductase (DHDPR) is an important enzyme which is involved in the biosynthetic pathway that leads to the production of L‐lysine in bacteria. In order to design potent inhibitors against this enzyme, its detailed three‐dimensional structure is required. DHDPR from A. baumannii ( Ab DHDPR) has been cloned, expressed, purified and crystallized. Here, the preliminary X‐ray crystallographic data of Ab DHDPR are reported. The crystals were grown using the hanging‐drop vapour‐diffusion method with PEG 3350 as the precipitating agent The crystals belonged to the orthorhombic space group P 222, with unit‐cell parameters a = 80.0, b = 100.8, c = 147.6 Å, and contained four molecules in the asymmetric unit. The complete structure determination of Ab DHDPR is in progress.