MSK
Search
- Page Path
- HOME > Search
Research Support, Non-U.S. Gov'ts
- 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
- 47 View
- 0 Download
- 7 Crossref
-
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.
-
Citations
Citations to this article as recorded by
- Expression, Characterisation, Homology Modelling and Molecular Docking of a Novel M17 Family Leucyl-Aminopeptidase from Bacillus cereus CZ
Jie Liu, Tangbing Cui
International Journal of Molecular Sciences.2023; 24(21): 15939. CrossRef - Screening and verification for proteins that interact with leucine aminopeptidase of Taenia pisiformis using a yeast two-hybrid system
Shaohua Zhang
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
Thien-Hoang Ho, Myoung-Ki Hong, Seunghwan Kim, Jeong-Gu Kim, Jongha Lee, Kyoungho Jung, Inho Lee, Munyoung Choi, Hyunjae Park, Sanghee Lee, Yeh-Jin Ahn, Lin-Woo Kang
Crop and Pasture Science.2017; 68(5): 434. CrossRef - An angiotensin-converting enzyme-inhibitory metabolite with partial structure of microginin in a cyanobacterium Anabaena fertilissima CCC597, producing fibrinolytic protease
Suvendra Nath Bagchi, Shobha Sondhia, Manish Kumar Agrawal, Sonali Banerjee
Journal of Applied Phycology.2016; 28(1): 177. CrossRef - Structure and Substrate Recognition of the Bottromycin Maturation Enzyme BotP
Greg Mann, Liujie Huo, Sebastian Adam, Brunello Nardone, Jeremie Vendome, Nicholas James Westwood, Rolf Müller, Jesko Koehnke
ChemBioChem.2016; 17(23): 2286. CrossRef - Crystal Structures of Peptide Deformylase from Rice Pathogen Xanthomonas oryzae pv. oryzae in Complex with Substrate Peptides, Actinonin, and Fragment Chemical Compounds
Ho-Phuong-Thuy Ngo, Thien-Hoang Ho, Inho Lee, Huyen-Thi Tran, Bookyo Sur, Seunghwan Kim, Jeong-Gu Kim, Yeh-Jin Ahn, Sun-Shin Cha, Lin-Woo Kang
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
Huyen-Thi Tran, Tan-Viet Pham, Ho-Phuong-Thuy Ngo, Myoung-Ki Hong, Jeong-Gu Kim, Sang Hee Lee, Yeh-Jin Ahn, Lin-Woo Kang
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
- Characterization of Thermostable Deblocking Aminopeptidases of Archaeon Thermococcus onnurineus NA1 by Proteomic and Biochemical Approaches
- Yeol Gyun Lee , Sun-Hee Leem , Young-Ho Chung , Seung Il Kim
- J. Microbiol. 2012;50(5):792-797. Published online November 4, 2012
- DOI: https://doi.org/10.1007/s12275-012-2461-2
- 38 View
- 0 Download
- 2 Scopus
-
Abstract
- Thermococcus onnurineus NA1 is a hyperthermophilic archaeon that grows optimally at >80°C. The deblocking aminopeptidase (DAP) (TNA1-DAP1) encoded in Ton_1032 of T. onnurineus NA1 is considered a major DAP. However, four genes encoding putative DAP have been identified from a genomic analysis of T. onnurineus NA1. A proteomic analysis revealed that all four DAPs were differentially induced in YPS culture medium and, particularly, two DAPs (TNA1-DAP1 and TNA1-DAP2) were dominantly expressed in T. onnurineus NA1. The biochemical properties and enzyme activity of DAPs induced in an E. coli expression system suggested that the two major DAPs play complementary roles in T. onnurineus NA1.
First
Prev
TOP
