Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity

Tools
- Tools
+ Tools

Izoré, Thierry, Candace Ho, Y T, Kaczmarski, Joe A, Gavriilidou, Athina, Chow, Ka Ho, Steer, David L, Goode, Robert J A, Schittenhelm, Ralf B, Tailhades, Julien, Tosin, Manuela, Challis, Gregory L., Krenske, Elizabeth H, Ziemert, Nadine, Jackson, Colin J and Cryle, Max J (2021) Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity. Nature Communications, 12 (1). 2511. doi:10.1038/s41467-021-22623-0 ISSN 2041-1723.

Research output not available from this repository.

Request-a-Copy directly from author or use local Library Get it For Me service.

Official URL: https://doi.org/10.1038/s41467-021-22623-0

Request Changes to record.

Abstract

Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a peptide bond between two peptidyl carrier protein (PCP)-bound substrates. In this work, we report structural snapshots of a condensation domain in complex with an aminoacyl-PCP acceptor substrate. These structures allow the identification of a mechanism that controls access of acceptor substrates to the active site in condensation domains. The structures of this complex also allow us to demonstrate that condensation domain active sites do not contain a distinct pocket to select the side chain of the acceptor substrate during peptide assembly but that residues within the active site motif can instead serve to tune the selectivity of these central biosynthetic domains.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
SWORD Depositor: Library Publications Router
Journal or Publication Title: Nature Communications
Publisher: Nature Publishing Group
ISSN: 2041-1723
Official Date: 4 May 2021
Dates:
DateEvent
4 May 2021Published
23 March 2021Accepted
Volume: 12
Number: 1
Article Number: 2511
DOI: 10.1038/s41467-021-22623-0
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Is Part Of: 1

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us