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- Crystal Structure of XoLAP, a Leucine Aminopeptidase, from Xanthomonas oryzae pv. oryzae
- Jin-Kwang Kim , Sampath Natarajan , Hanseul Park , Kim-Hung Huynh , Sang Hee Lee , Jeong-Gu Kim , Yeh-Jin Ahn , Lin-Woo Kang
- J. Microbiol. 2013;51(5):627-632. Published online October 31, 2013
- DOI: https://doi.org/10.1007/s12275-013-3234-2
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Abstract
- Aminopeptidases are metalloproteinases that degrade N-terminal residues from protein and play important roles in cell growth and development by controlling cell homeostasis and protein maturation. We determined the crystal structure of XoLAP, a leucyl aminopeptidase, at 2.6 Å resolution from Xanthomonas oryzae pv. oryzae, causing the destructive rice disease of bacterial blight. It is the first crystal structure of aminopeptidase from phytopathogens as a drug target. XoLAP existed as a hexamer and the monomer structure consisted of an N-terminal cap domain and a C-terminal peptidase domain with two divalent zinc ions. XoLAP structure was compared with BlLAP and EcLAP (EcPepA) structures. Based on the structural comparison, the molecular model of XoLAP in complex with the natural aminopeptidase inhibitor of microginin FR1 was proposed. The model structure will be useful to develop a novel antibacterial drug against Xoo.
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Citations
Citations to this article as recorded by
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Parasitology Research.2019; 118(12): 3387. CrossRef - Transcriptional expression of aminoacyl tRNA synthetase genes of Xanthomonas oryzae pv. oryzae (Xoo) on rice-leaf extract treatment and crystal structure of Xoo glutamyl-tRNA synthetase
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Journal of Agricultural and Food Chemistry.2016; 64(39): 7307. CrossRef - Crystallization and preliminary X-ray crystallographic analysis of the XoGroEL chaperonin fromXanthomonas oryzaepv.oryzae
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Acta Crystallographica Section F Structural Biology Communications.2014; 70(5): 604. CrossRef
- Expression, Characterisation, Homology Modelling and Molecular Docking of a Novel M17 Family Leucyl-Aminopeptidase from Bacillus cereus CZ
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