Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872056 | FEBS Letters | 2010 | 5 Pages |
Abstract
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 2.1Â Ã
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.
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Authors
Seung Kon Hong, Kook Han Kim, Joon Kyu Park, Ki-Woong Jeong, Yangmee Kim, Eunice EunKyeong Kim,