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 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 A resolution and belonged to the cubic space group P2(1)3. The unit-cell volume of the crystal was compatible with the presence of two monomers in the asymmetric unit.
Huynh
Kim-Hung
KH
Department of Advanced Technology Fusion, Konkuk University, Seoul, Republic of Korea.
Natarajan
Sampath
S
Choi
Jeongyoon
J
Song
Na-Hyun
NH
Kim
Jeong-Gu
JG
Lee
Byoung-Moo
BM
Ahn
Yeh-Jin
YJ
Kang
Lin-Woo
LW
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D005798:Genes, Bacterial; D007931:Leucyl Aminopeptidase / Q000737:chemistry*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D014974:Xanthomonas / Q000201:enzymology* / Q000235:genetics*
D007931:Leucyl Aminopeptidase