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

doi:10.1007/s12275-013-3234-2

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Research Support, Non-U.S. Gov't
Crystal Structure of XoLAP, a Leucine Aminopeptidase, from Xanthomonas oryzae pv. oryzae: Jin-Kwang Kim ¹, Sampath Natarajan ¹, Hanseul Park ², Kim-Hung Huynh ¹, Sang Hee Lee ³, Jeong-Gu Kim ⁴, Yeh-Jin Ahn ², Lin-Woo Kang ^1,5; Journal of Microbiology 2013;51(5):627-632.
DOI: https://doi.org/10.1007/s12275-013-3234-2
Published online: October 31, 2013

¹Department of Biological Sciences, Konkuk University, Seoul 143-701, Republic of Korea, ²Department of Green Life Science, College of Convergence, Sangmyung University, Seoul 110-743, Republic of Korea, ³3Drug Resstance Proteomics Laboratory, Department of Biological Sciences, Myongji University, Yongin 449-728, Republic of Korea, ⁴Microbial Genetics Division, National Institute of Agricultural Biotechnology (NIAB), Rural Development Administration (RDA), Suwon 441-707, Republic of Korea, ⁵Protein and Chemical Inc., Seoul 143-701, Republic of Korea¹Department of Biological Sciences, Konkuk University, Seoul 143-701, Republic of Korea, ²Department of Green Life Science, College of Convergence, Sangmyung University, Seoul 110-743, Republic of Korea, ³3Drug Resstance Proteomics Laboratory, Department of Biological Sciences, Myongji University, Yongin 449-728, Republic of Korea, ⁴Microbial Genetics Division, National Institute of Agricultural Biotechnology (NIAB), Rural Development Administration (RDA), Suwon 441-707, Republic of Korea, ⁵Protein and Chemical Inc., Seoul 143-701, Republic of Korea

Corresponding author: Yeh-Jin Ahn , Tel: +82-2-450-4090,
Lin-Woo Kang , Tel: +82-2-450-4090,

Received: 22 April 2013 • Accepted: 17 May 2013

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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.

Keywords: aminopeptidase;Xanthomonas oryzae pv. oryzae (Xoo);microginin FR1;crystal structure;drug target

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Crystal Structure of XoLAP, a Leucine Aminopeptidase, from Xanthomonas oryzae pv. oryzae

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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