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

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 h...

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Bibliographic Details
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
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Summary: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.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309109031467