We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
New design platform for malonyl-CoA-acyl carrier protein transacylase
- Authors
Hong, Seung Kon; Kim, Kook Han; Park, Joon Kyu; Jeong, Ki-Woong; Kim, Yangmee; Kim, Eunice EunKyeong
- Abstract
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 2.1Å 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.
- Subjects
CARRIER proteins; ACYLTRANSFERASES; FATTY acids; BIOSYNTHESIS; ANTIBACTERIAL agents; MOLECULAR structure; STREPTOCOCCUS pneumoniae; COENZYMES
- Publication
FEBS Letters, 2010, Vol 584, Issue 6, p1240
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2010.02.038