| Title | Crystal Structure of XoLAP, a Leucine Aminopeptidase, from Xanthomonas oryzae pv. oryzae |
|---|---|
| Author | Jin-Kwang Kim1, Sampath Natarajan1, Hanseul Park2, Kim-Hung Huynh1, Sang Hee Lee3, Jeong-Gu Kim4, Yeh-Jin Ahn2*, and Lin-Woo Kang1,5* |
| Address | 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 Korea |
| Bibliography | Journal of Microbiology, 51(5),627-632, 2013, |
| DOI | 10.1007/s12275-013-3234-2 |
| Key Words | aminopeptidase, Xanthomonas oryzae pv. oryzae (Xoo), microginin FR1, crystal structure, drug target |
| 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. |