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KMID : 0578320120330010019
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Molecules and Cells
2012 Volume.33 No. 1 p.19 ~ p.25
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Crystal Structure of Malonyl CoA-Acyl Carrier Protein Transacylase from Xanthomanous oryzae pv. oryzae and Its Proposed Binding with ACP
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Sampath Natarajan
Kim Jin-Kwang
Jung Tae-Kyun
Ho-Phuong-Thuy Ngo
Hong Myoung-Ki
Kim Seung-Hwan
Viet Pham Tan
Ahn Seok-Joon
Lee Sang-Hee
Han Ye-Sun
Ahn Yeh-Jin
Kang Lin-Woo
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Abstract
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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 A 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.
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KEYWORD
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acyl carrier protein, computational docking, fatty acid synthesis, malonyl CoA-acyl carrier protein transacylase, Xanthomanous oryzae pv. oryzae
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