Open AccessExpression, crystallization and preliminary X‐ray crystallographic analysis of Xoo0352, d ‐alanine‐ d ‐alanine ligase A, from Xanthomonas oryzae pv. oryzae
Author(s) -
Doan Thanh Thi Ngoc,
Kim JinKwang,
Kim Hyesoon,
Ahn YehJin,
Kim JeongGu,
Lee ByoungMoo,
Kang LinWoo
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108028820
Subject(s) - xanthomonas oryzae , dna ligase , xanthomonas oryzae pv. oryzae , molecular replacement , alanine , brachypodium distachyon , biochemistry , escherichia coli , chemistry , stereochemistry , crystallography , enzyme , gene , amino acid , genome
Xanthomonas oryzae pv. oryzae (Xoo) causes bacterial blight (BB), which is one of the most devastating diseases of rice in most rice‐growing countries. d ‐Alanine‐ d ‐alanine ligase A (DdlA), coded by the Xoo0352 gene, was expressed, purified and crystallized. DdlA is an enzyme that is involved in d ‐alanine metabolism and the biosynthesis of an essential bacterial peptidoglycan precursor, in which it catalyzes the formation of d ‐alanyl‐ d ‐alanine from two d ‐alanines, and is thus an attractive antibacterial drug target against Xoo. The DdlA crystals diffracted to 2.3 Å resolution and belonged to the primitive tetragonal space group P 4 3 2 1 2, with unit‐cell parameters a = b = 83.0, c = 97.6 Å. There is one molecule in the asymmetric unit, with a corresponding V M of 1.88 Å 3 Da −1 and a solvent content of 34.6%. The initial structure was determined by molecular replacement using d ‐alanine‐ d ‐alanine ligase from Staphylococcus aureus (PDB code 2i87 ) as a template model.