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Mol. Cells 2012; 33(1): 19-25
Published online November 29, 2011
https://doi.org/10.1007/s10059-012-2155-y
© The Korean Society for Molecular and Cellular Biology
Crystal Structure of Malonyl CoA-Acyl Carrier Protein Transacylase from Xanthomanous oryzae pv. oryzae and Its Proposed Binding with ACP
Correspondence to : *Correspondence: lkang@konkuk.ac.kr (LWK); yjahn@smu.ac.kr (YJA)
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 ? 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.
Keywords acyl carrier protein, computational docking, fatty acid synthesis, malonyl CoA-acyl carrier protein transacylase, Xanthomanous oryzae pv. oryzae
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Research Article
Mol. Cells 2012; 33(1): 19-25
Published online January 31, 2012 https://doi.org/10.1007/s10059-012-2155-y
Copyright © The Korean Society for Molecular and Cellular Biology.
Crystal Structure of Malonyl CoA-Acyl Carrier Protein Transacylase from Xanthomanous oryzae pv. oryzae and Its Proposed Binding with ACP
Sampath Natarajan1,6, Jin-Kwang Kim1,6, Tae-Kyun Jung1, Thanh Thi Ngoc Doan1, Ho-Phuong-Thuy Ngo1, Myoung-Ki Hong1, Seunghwan Kim1, Viet Pham Tan1, Seok Joon Ahn1,2, Sang Hee Lee3, Yesun Han1, Yeh-Jin Ahn4,*, and Lin-Woo Kang1,5,*
1Department of Advanced Technology Fusion, Konkuk University, Seoul 143-701, Korea, 2Department of Applied Biology and Chemistry, College of Agriculture and Life Sciences, Seoul National University, Seoul 151-921, Korea, 3Department of Biological Sciences, Myongji University, Yongin 449-728, Korea, 4Department of Green Life Science, College of Convergence, Sangmyung University, Seoul 110-743, Korea, 5Center for Biotechnology Research in UBITA (CBRU), Seoul 143-701, Korea, 6These authors contributed equally to this work.
Correspondence to:*Correspondence: lkang@konkuk.ac.kr (LWK); yjahn@smu.ac.kr (YJA)
Abstract
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 ? 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.
Keywords: acyl carrier protein, computational docking, fatty acid synthesis, malonyl CoA-acyl carrier protein transacylase, Xanthomanous oryzae pv. oryzae
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