PXD024004-1

PXD024004 is an original dataset announced via ProteomeXchange.

Title	Understanding condensation domain selectivity in non-ribosomal peptide biosynthesis: structural characterization of the acceptor bound state
Description	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 the first 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 previously uncharacterized 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.
HostingRepository	PRIDE
AnnounceDate	2021-05-28
AnnouncementXML	Submission_2021-05-28_04:35:11.209.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	David Steer
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	No PTMs are included in the dataset
Instrument	micrOTOF II

Revision	Datetime	Status	ChangeLog Entry
0	2021-02-04 23:09:44	ID requested
⏵ 1	2021-05-28 04:35:12	announced

Izor, é T, Candace Ho YT, Kaczmarski JA, Gavriilidou A, Chow KH, Steer DL, Goode RJA, Schittenhelm RB, Tailhades J, Tosin M, Challis GL, Krenske EH, Ziemert N, Jackson CJ, Cryle MJ, Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity. Nat Commun, 12(1):2511(2021) [pubmed]

submitter keyword: Non-ribosomal peptide

Biosynthesis

Condensation domain

Peptidyl carrier protein

Biocatalysis

Max Cryle
contact affiliation	Biomedicine Discovery Institute, Monash University, Clayton 3800, Victoria, Australia
contact email	max.cryle@monash.edu
lab head
David Steer
contact affiliation	Biomedicine Discovery Institute, Monash University, Clayton 3800, Victoria, Australia
contact email	david.steer@monash.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/05/PXD024004

PRIDE project URI

• PRIDE
  1. PXD024004
     1. Label: PRIDE project
     2. Name: Understanding condensation domain selectivity in non-ribosomal peptide biosynthesis: structural characterization of the acceptor bound state