3IM9
Crystal structure of MCAT from Staphylococcus aureus
Summary for 3IM9
| Entry DOI | 10.2210/pdb3im9/pdb |
| Related | 3IM8 |
| Descriptor | Malonyl CoA-acyl carrier protein transacylase, CALCIUM ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | fatty acid synthesis, malonyl-coa: acyl carrier protein transacylase (mcat), fabd, staphylococcus aureus, acyltransferase, fatty acid biosynthesis, lipid synthesis, transferase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 34679.27 |
| 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 Cited by 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: 20176020DOI: 10.1016/j.febslet.2010.02.038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
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