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Ho-Phuong-Thuy Ngo,Diem-Quynh Nguyen,김승환,김정구,안예진,강린우 한국구조생물학회 2019 Biodesign Vol.7 No.2
Xanthomonas oryzae pv. oryzae (Xoo) is a plant pathogen, which causes a bacterial blight of rice. The bacterial blightis one of the most devastating diseases of rice in most of the rice growing countries and there is no effective pesticideagainst bacterial blight. The β-ketoacyl-acyl carrier protein synthase III (FabH) plays a key role in fatty acid synthesis(FAS) and is a promising drug target for the development of antibacterial agents. Xoo0878 gene, a fabH gene, from Xoowas cloned and its gene product Xoo0878 was expressed, purified and crystallized. Xoo0878 crystal diffracted to 2.1Åresolution and belonged to the triclinic space group P1, with unit-cell parameters a = 57.3Å, b = 64.7Å, c = 104.2Å and α =81.6°, β = 84.7°, γ = 74.4°. There are four monomers in the asymmetric unit, with a corresponding crystal volume per proteinweight of 2.65 Å3 Da−1 and a solvent content of 53.6%. Xoo0878 structure will be useful to develop new antibacterial agentsagainst Xoo.
Conformational change of organic cofactor PLP is essential for catalysis in PLP-dependent enzymes
Ho-Phuong-Thuy Ngo,Diem-Quynh Nguyen,Hyunjae Park,Yoon Sik Park,Kiwoong Kwak,Taejoon Kim,Jang Ho Lee,Kyoung Sang Cho,강린우 생화학분자생물학회 2022 BMB Reports Vol.55 No.9
Pyridoxal 5’-phosphate (PLP)-dependent enzymes are ubiquitous,catalyzing various biochemical reactions of approximately 4%of all classified enzymatic activities. They transform amines andamino acids into important metabolites or signaling moleculesand are important drug targets in many diseases. In the crystalstructures of PLP-dependent enzymes, organic cofactor PLPshowed diverse conformations depending on the catalytic step. The conformational change of PLP is essential in the catalyticmechanism. In the study, we review the sophisticated catalyticmechanism of PLP, especially in transaldimination reactions. Most drugs targeting PLP-dependent enzymes make a covalentbond to PLP with the transaldimination reaction. A detailedunderstanding of organic cofactor PLP will help develop a newdrug against PLP-dependent enzymes.
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
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.