Details

Autor(en) / Beteiligte

• Sampath Natarajan, Konkuk University, Seoul, Republic of Korea
• Kim, J.K., Konkuk University, Seoul, Republic of Korea
• Jung, T.K., Konkuk University, Seoul, Republic of Korea
• Thanh Thi Ngoc Doan, Konkuk University, Seoul, Republic of Korea
• Ho-Phuong-Thuy Ngo, Konkuk University, Seoul, Republic of Korea
• Hong, M.K., Konkuk University, Seoul, Republic of Korea
• Kim, S.H., Konkuk University, Seoul, Republic of Korea
• Viet Pham Tan, Konkuk University, Seoul, Republic of Korea
• Ahn, S.J., Konkuk University, Seoul, Republic of Korea
• Lee, S.H., Myongji University, Yongin, Republic of Korea
• Han, Y.S., Konkuk University, Seoul, Republic of Korea
• Ahn, Y.J., Sangmyung University, Seoul, Republic of Korea
• Kang, L.W., Konkuk University, Seoul, Republic of Korea

Titel

Crystal structure of malonyl CoA-Acyl carrier protein transacylase from Xanthomanous oryzae pv. oryzae and its proposed binding with ACP

Ist Teil von

• Molecules and Cells, 2012, 33(1), , pp.19-25

Ort / Verlag

Springer: Korean Society for Molecular and Cellular Biology

Erscheinungsjahr

2012

Link zum Volltext

Quelle

SpringerLink (Online service)

Beschreibungen/Notizen

• 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 angstrom 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.