New design platform for malonyl-CoA-acyl carrier protein transacylase.

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 Lett

journal_title

FEBS letters

authors

Hong SK,Kim KH,Park JK,Jeong KW,Kim Y,Kim EE

doi

10.1016/j.febslet.2010.02.038

subject

Has Abstract

pub_date

2010-03-19 00:00:00

pages

1240-4

issue

6

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(10)00142-0

journal_volume

584

pub_type

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