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Sampath Natarajan,강린우,김진광,Tae-Kyun Jung,Thanh Thi Ngoc Doan,Ho-Phuong-Thuy Ngo,홍명기,Seunghwan Kim,Viet Pham Tan,Seok Joon Ahn,이상희,한예선,안예진 한국분자세포생물학회 2012 Molecules and cells Vol.33 No.1
Xanthomonas oryzae pv. oryzae (Xoo) is a plant bacterial pathogen that causes bacterial blight (BB) disease, resulting in serious production losses of rice. The crystal structure of malonyl CoA-acyl carrier protein transacylase (XoMCAT), encoded by the gene fabD (Xoo0880) from Xoo, was determined at 2.3 Å resolution in complex with N-cyclohexyl-2-aminoethansulfonic acid. Malonyl CoA-acyl carrier protein transacylase transfers malonyl group from malonyl CoA to acyl carrier protein (ACP). The transacylation step is essential in fatty acid synthesis. Based on the rationale, XoMCAT has been considered as a target for antibacterial agents against BB. Protein-protein interaction between XoMCAT and ACP was also extensively investigated using computational docking, and the proposed model revealed that ACP bound to the cleft between two XoMCAT subdomains.
Crystal Structure of XoLAP, a Leucine Aminopeptidase, from Xanthomonas oryzae pv. oryzae
김진광,Sampath Natarajan,박한슬,Kim-Hung Huynh,이상희,김정구,안예진,강린우 한국미생물학회 2013 The journal of microbiology Vol.51 No.5
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.
Structural Proteomic Study of Xanthomonas oryzae pv. oryzae to Develop a Novel Antibacterial Drug
Dong Wook Kim,Phuong Thuy Ho Ngo,Thanh Thi Ngoc Doan,Natarajan Sampath,Jin Kwang Kim,Jae Wook Jung,Myoung Ki Hong,Junho Jung,Seung Hwan Kim,Hye Soon Kim,Hung Kim,Yeh Jin Ahn,Jeong G 한국응용생명화학회 2008 Applied Biological Chemistry (Appl Biol Chem) Vol.51 No.5