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Expression, crystallization and preliminary X-ray crystallographic analysis of D-alanine-D-alanine ligase from OXA-23-producing Acinetobacter baumannii K0420859.

Authors :
Huynh KH
Tran HT
Pham TV
Ngo HP
Cha SS
Chung KM
Lee SH
Kang LW
Source :
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2014 Apr; Vol. 70 (Pt 4), pp. 505-8. Date of Electronic Publication: 2014 Mar 25.
Publication Year :
2014

Abstract

Acinetobacter baumannii causes bacteraemia, pneumonia, other respiratory-tract and urinary-tract infections in humans. OXA-23 carbapenemase-producing A. baumannii K0420859 (A. baumannii OXA-23) is resistant to carbapenem, a common antibacterial drug. To develop an efficient and novel antibacterial drug against A. baumannii OXA-23, D-alanine-D-alanine ligase, which is essential in bacterial cell-wall synthesis, is of interest. Here, the D-alanine-D-alanine ligase (AbDdl) gene from A. baumannii OXA-23 was cloned and expressed, and the AbDdl protein was purified and crystallized; this enzyme can be used as a novel target for an antibacterial drug against A. baumannii OXA-23. The AbDdl crystal diffracted to a resolution of 2.8 Šand belonged to the orthorhombic space group P212121, with unit-cell parameters a = 113.4, b = 116.7, c = 176.5 Å, a corresponding VM of 2.8 Å(3) Da(-1) and a solvent content of 56.3%, and six protomers in the asymmetric unit.

Details

Language :
English
ISSN :
2053-230X
Volume :
70
Issue :
Pt 4
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology communications
Publication Type :
Academic Journal
Accession number :
24699750
Full Text :
https://doi.org/10.1107/S2053230X14005081