3IM8

Crystal structure of MCAT from Streptococcus pneumoniae

Summary for 3IM8

• Entry DOI: 10.2210/pdb3im8/pdb
• Related: 3IM9
• Descriptor: Malonyl acyl carrier protein transacylase, ACETATE ION (3 entities in total)
• Functional Keywords: fatty acid synthesis, malonyl-coa, acyl carrier protein transacylase (mcat), fabd, acyltransferase, transferase
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 33307.93

Authors

Hong, S.K.,Kim, K.H.,Park, J.K.,Kim, Y.M.,Kim, E.E. (deposition date: 2009-08-10, release date: 2010-06-16, Last modification date: 2023-11-01)

Primary citation

Hong, S.K.,Kim, K.H.,Park, J.K.,Jeong, K.-W.,Kim, Y.M.,Kim, E.E.
New design platform for malonyl-CoA-acyl carrier protein transacylase
Febs Lett., 584:1240-1244, 2010

PubMed 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.

PubMed: 20176020
DOI: 10.1016/j.febslet.2010.02.038

Experimental method

X-RAY DIFFRACTION (2.1 Å)