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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
Author(s) -
Huynh KimHung,
Tran HuyenThi,
Pham TanViet,
Ngo HoPhuongThuy,
Cha SunShin,
Chung Kyung Min,
Lee Sang Hee,
Kang LinWoo
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14005081
Subject(s) - acinetobacter baumannii , dna ligase , cephem , microbiology and biotechnology , chemistry , escherichia coli , alanine , carbapenem , antibiotics , stereochemistry , biology , biochemistry , bacteria , enzyme , gene , amino acid , pseudomonas aeruginosa , carboxylic acid , genetics
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 Ab Ddl protein was purified and crystallized; this enzyme can be used as a novel target for an antibacterial drug against A. baumannii OXA‐23. The Ab Ddl crystal diffracted to a resolution of 2.8 Å and belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 113.4, b = 116.7, c = 176.5 Å, a corresponding V M of 2.8 Å 3 Da −1 and a solvent content of 56.3%, and six protomers in the asymmetric unit.