6AD3
Structural characterization of the condensation domain from Monacolin K polyketide synthase MokA
Summary for 6AD3
| Entry DOI | 10.2210/pdb6ad3/pdb |
| Descriptor | Lovastatin nonaketide synthase mokA (2 entities in total) |
| Functional Keywords | polyketide synthease, condensation domain, nonribosomal peptide synthetases, biosynthetic protein |
| Biological source | Monascus pilosus (Red mold) |
| Total number of polymer chains | 1 |
| Total formula weight | 57446.18 |
| Authors | |
| Primary citation | Wang, L.,Yuan, M.,Zheng, J. Crystal structure of the condensation domain from lovastatin polyketide synthase. Synth Syst Biotechnol, 4:10-15, 2019 Cited by PubMed Abstract: The highly reducing iterative polyketide synthases responsible for lovastatin biosynthesis contains a section homologous to condensation (CON) domain observed in nonribosomal peptide synthetases (NRPSs). In the present study, we expressed the isolated lovastatin CON domain and solved the crystal structure to 1.79 Å resolution. The overall structure shows similarity to canonical condensation domains of NRPSs, containing the N-terminal and C-terminal subdomains that resemble enzymes of chloramphenicol acetyltransferase family, whereas distinct structural features are observed at the active site. The acceptor entry of the substrate channel is blocked by a flexible loop, thereby preventing the loading of substrate for a new round of chain elongation. The mutation of conserved catalytic motif located at the midpoint of substrate channel agrees with the incapability of CON to catalyzed amide-bond formation. The structure helps to understand the function of CON in lovastatin biosynthesis. PubMed: 30533541DOI: 10.1016/j.synbio.2018.11.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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