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 2.1A 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hong SK,Kim KH,Park JK,Jeong KW,Kim Y,Kim EEdoi
10.1016/j.febslet.2010.02.038subject
Has Abstractpub_date
2010-03-19 00:00:00pages
1240-4issue
6eissn
0014-5793issn
1873-3468pii
S0014-5793(10)00142-0journal_volume
584pub_type
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