5WM7
Crystal Structure of CahJ in Complex with AMP
Summary for 5WM7
| Entry DOI | 10.2210/pdb5wm7/pdb |
| Descriptor | Salicylate-AMP ligase, ADENOSINE MONOPHOSPHATE, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | ligase, adenylation domain, peptide synthetase |
| Biological source | Streptomyces gandocaensis |
| Total number of polymer chains | 1 |
| Total formula weight | 61281.89 |
| Authors | Sikkema, A.P.,Smith, J.L. (deposition date: 2017-07-28, release date: 2018-05-23, Last modification date: 2023-10-04) |
| Primary citation | Tripathi, A.,Park, S.R.,Sikkema, A.P.,Cho, H.J.,Wu, J.,Lee, B.,Xi, C.,Smith, J.L.,Sherman, D.H. A Defined and Flexible Pocket Explains Aryl Substrate Promiscuity of the Cahuitamycin Starter Unit-Activating Enzyme CahJ. Chembiochem, 19:1595-1600, 2018 Cited by PubMed Abstract: Cahuitamycins are biofilm inhibitors assembled by a convergent nonribosomal peptide synthetase pathway. Previous genetic analysis indicated that a discrete enzyme, CahJ, serves as a gatekeeper for cahuitamycin structural diversification. Here, the CahJ protein was probed structurally and functionally to guide the formation of new analogues by mutasynthetic studies. This analysis enabled the in vivo production of a new cahuitamycin congener through targeted precursor incorporation. PubMed: 29742306DOI: 10.1002/cbic.201800233 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.777 Å) |
Structure validation
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