Hong, Seung Kon Kim, Kook Han Park, Joon Kyu Jeong, Ki-Woong Kim, Yangmee Kim, Eunice EunKyeong 2024-01-20T19:33:56Z 2024-01-20T19:33:56Z 2021-09-02 2010-03-19 0014-5793 https://pubs.kist.re.kr/handle/201004/131628 Malonyl-CoA-acyl carrier protein transacylase (MCAT) transfers the malonyl group from malonyl-CoA to holo-acyl carrier protein (ACP), and since malonyl-ACP is a key building block for fatty-acid biosynthesis it is considered as a promising antibacterial target. The crystal structures of MCAT from Staphylococcus aureus and Streptococcus pneumoniae have been determined at 1.46 and 2.1 angstrom resolution, respectively. In the SaMCAT structure, the N-terminal expression peptide of a neighboring molecule running in the opposite direction of malonyl-CoA makes extensive interactions with the highly conserved "Gly-Gln-Gly-Ser-Gln" stretch, suggesting a new design platform. Mutagenesis results suggest that Ser91 and His199 are the catalytic dyad. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. English WILEY FATTY-ACID BIOSYNTHESIS STREPTOMYCES-COELICOLOR CRYSTAL-STRUCTURE ACP TRANSACYLASE MCAT TARGETS SITE New design platform for malonyl-CoA-acyl carrier protein transacylase Article 10.1016/j.febslet.2010.02.038 1 FEBS LETTERS, v.584, no.6, pp.1240 - 1244 FEBS LETTERS 584 6 1240 1244 scie scopus 000275738700028 2-s2.0-77950368619 Biochemistry & Molecular Biology Biophysics Cell Biology Biochemistry & Molecular Biology Biophysics Cell Biology Article FATTY-ACID BIOSYNTHESIS STREPTOMYCES-COELICOLOR CRYSTAL-STRUCTURE ACP TRANSACYLASE MCAT TARGETS SITE Fatty-acid biosynthesis FabD MCAT Antibacterial Structure based drug design