5WM5

Crystal Structure of CahJ in Complex with 5-Methylsalicyl Adenylate

Summary for 5WM5

Entry DOI	10.2210/pdb5wm5/pdb
Descriptor	Salicylate-AMP ligase, 9-(5-O-{(S)-hydroxy[(2-hydroxy-5-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine, ACETATE ION, ... (5 entities in total)
Functional Keywords	ligase, adenylation domain, peptide synthetase
Biological source	Streptomyces gandocaensis
Total number of polymer chains	1
Total formula weight	61475.06
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: 29742306 DOI: 10.1002/cbic.201800233 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.797 Å)

Structure validation