Cloning, expression, crystallization and preliminary structural studies of dihydrodipicolinate reductase from Acinetobacter baumannii. Issue 6 (31st May 2013)

• Record Type: Journal Article
• Authors: Kaushik, Sanket; Singh, Avinash; Sinha, Mau; Kaur, Punit; Sharma, Sujata; Singh, Tej P.
• Is Part Of: Acta crystallographica. Volume 69:Issue 6(2013:Jun.)
• Page Start: 653
• Page End: 656
• Publication Date: 2013-05-31
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113011214
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>Acinetobacter baumannii</italic> 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 <italic>A. baumannii</italic> 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 <italic>A. baumannii</italic> (<italic>Ab</italic>DHDPR) has been cloned, expressed, purified and crystallized. Here, the preliminary X‐ray crystallographic data of <italic>Ab</italic>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 <italic>P</italic>222, with unit‐cell parameters <italic>a</italic> = 80.0, <italic>b</italic> = 100.8, <italic>c</italic> = 147.6 Å, and contained four molecules in the asymmetric unit. The complete structure determination of <italic>Ab</italic>DHDPR is in progress.</p> </abstract>