Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of leucine aminopeptidase (LAP) from the pepA gene of Xanthomonas oryzae pv. oryzae

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2009-09, Vol.65 (9), p.952-955
• Main Authors: Huynh, Kim-Hung, Natarajan, Sampath, Choi, Jeongyoon, Song, Na-Hyun, Kim, Jeong-Gu, Lee, Byoung-Moo, Ahn, Yeh-Jin, Kang, Lin-Woo
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Cloning, Molecular; Crystallization; Crystallization Communications; Crystallography, X-Ray; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Genes, Bacterial; leucine aminopeptidase; Leucyl Aminopeptidase - chemistry; Molecular Sequence Data; Oryza sativa; Sequence Alignment; Xanthomonas - enzymology; Xanthomonas - genetics; Xanthomonas oryzae; Xanthomonas oryzae pv. oryzae
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309109031467

Xanthomonas oryzae pv. oryzae (Xoo) causes the serious disease bacterial blight in rice. The pepA (Xoo0834) gene from Xoo is one of around 100 genes that have been selected for the design of antibacterial drugs. The pepA gene encodes leucine aminopeptidase (LAP), an exopeptidase that catalyzes the hydrolysis of leucine residues from the N‐terminus of a protein or peptide. This enzyme was expressed in Escherichia coli, purified and crystallized, and preliminary X‐ray structural studies have been carried out. The LAP crystal diffracted to 2.6 Å resolution and belonged to the cubic space group P213. The unit‐cell volume of the crystal was compatible with the presence of two monomers in the asymmetric unit.