3im8

Publication Abstract from PubMed

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 2.1A 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.

New design platform for malonyl-CoA-acyl carrier protein transacylase.,Hong SK, Kim KH, Park JK, Jeong KW, Kim Y, Kim EE FEBS Lett. 2010 Mar 19;584(6):1240-4. Epub 2010 Feb 19. PMID:20176020^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.