5WM3

Crystal Structure of CahJ in Complex with Salicyl Adenylate

Summary for 5WM3

• Entry DOI: 10.2210/pdb5wm3/pdb
• Descriptor: Salicylate-AMP ligase, 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: ligase, adenylation domain, peptide synthetase.
• Biological source: Streptomyces gandocaensis
• Total number of polymer chains: 1
• Total formula weight: 61636.48

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

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

Experimental method

X-RAY DIFFRACTION (1.679 Å)