PXD061798-1

PXD061798 is an original dataset announced via ProteomeXchange.

Title	Molecular basis for the phosphorylation of bacterial tyrosine kinase Wzc
Description	The regulation of polymerisation and translocation are of fundamental interest in biology. The Wzc class of integral membrane tyrosine autokinase proteins serve as the master regulators of the biosynthesis and export of some bacterial capsular and exopolysaccharides. These polysaccharides play essential roles in infection, defence, and some are important industrial products. Wzc monomers are comprised of a large periplasmic domain, two transmembrane helices and a C-terminal cytoplasmic kinase domain with a tyrosine-rich tail. Wzc functions through cycling the formation and dissociation of an octameric complex, driven by changes in the phosphorylation status of the tyrosine-rich tail. E. coli Wzc serves a model for the wider family and we have determined structures of intermediate states with different extents of phosphorylation. Structural and computational data reveal the pre-ordering of the tyrosine-rich tail, the molecular basis underlying the unidirectionality of phosphorylation events, and the underlying structural dynamics on how phosphorylation status is transmitted.
HostingRepository	PRIDE
AnnounceDate	2025-03-27
AnnouncementXML	Submission_2025-03-27_09:54:04.433.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Haigang Song
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	phosphorylated residue
Instrument	Orbitrap Eclipse

Revision	Datetime	Status	ChangeLog Entry
0	2025-03-13 08:32:08	ID requested
⏵ 1	2025-03-27 09:54:04	announced

Dataset with its publication pending

submitter keyword: Phosphorylation

Carol Robinson
contact affiliation	Kavli Institute for NanoScience Discovery, Dorothy Crowfoot Hodgkin Building, University of Oxford, OX1 3QU, United Kingdom Department of Chemistry, University of Oxford, OX1 3TA, United Kingdom
contact email	haigang.song@chem.ox.ac.uk
lab head
Haigang Song
contact affiliation	Department of Chemistry, University of oxford
contact email	haigang.song@chem.ox.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD061798
     1. Label: PRIDE project
     2. Name: Molecular basis for the phosphorylation of bacterial tyrosine kinase Wzc