8JBR
Structure of McyA2-CAPCP
Summary for 8JBR
| Entry DOI | 10.2210/pdb8jbr/pdb |
| Descriptor | McyA protein, ADENOSINE-5'-TRIPHOSPHATE, 4'-PHOSPHOPANTETHEINE, ... (4 entities in total) |
| Functional Keywords | nrpss, microcystin synthase, condensation domain, adenylation doamin, toxin |
| Biological source | Microcystis aeruginosa PCC 7806 |
| Total number of polymer chains | 1 |
| Total formula weight | 118202.93 |
| Authors | Peng, Y.J. (deposition date: 2023-05-09, release date: 2024-01-24, Last modification date: 2024-07-03) |
| Primary citation | Peng, Y.J.,Chen, Y.,Zhou, C.Z.,Miao, W.,Jiang, Y.L.,Zeng, X.,Zhang, C.C. Modular catalytic activity of nonribosomal peptide synthetases depends on the dynamic interaction between adenylation and condensation domains. Structure, 32:440-, 2024 Cited by PubMed Abstract: Nonribosomal peptide synthetases (NRPSs) are large multidomain enzymes for the synthesis of a variety of bioactive peptides in a modular and pipelined fashion. Here, we investigated how the condensation (C) domain and the adenylation (A) domain cooperate with each other for the efficient catalytic activity in microcystin NRPS modules. We solved two crystal structures of the microcystin NRPS modules, representing two different conformations in the NRPS catalytic cycle. Our data reveal that the dynamic interaction between the C and the A domains in these modules is mediated by the conserved "RXGR" motif, and this interaction is important for the adenylation activity. Furthermore, the "RXGR" motif-mediated dynamic interaction and its functional regulation are prevalent in different NRPSs modules possessing both the A and the C domains. This study provides new insights into the catalytic mechanism of NRPSs and their engineering strategy for synthetic peptides with different structures and properties. PubMed: 38340732DOI: 10.1016/j.str.2024.01.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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