1. Crystal structure of malonyl CoA-Acyl carrier protein transacylase from Xanthomanous oryzae pv. oryzae and its proposed binding with ACP.
- Author
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Natarajan S, Kim JK, Jung TK, Doan TT, Ngo HP, Hong MK, Kim S, Tan VP, Ahn SJ, Lee SH, Han Y, Ahn YJ, and Kang LW
- Subjects
- Acyl-Carrier Protein S-Malonyltransferase genetics, Acyl-Carrier Protein S-Malonyltransferase metabolism, Amino Acid Sequence, Bacterial Proteins genetics, Bacterial Proteins metabolism, Crystallization, Molecular Sequence Data, Acyl Carrier Protein metabolism, Acyl-Carrier Protein S-Malonyltransferase chemistry, Bacterial Proteins chemistry, Malonyl Coenzyme A metabolism, Xanthomonas enzymology
- 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 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.
- Published
- 2012
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