PXD068881-1

PXD068881 is an original dataset announced via ProteomeXchange.

Title	Study of the conformational dynamics of Helicobacter pylori CtpA
Description	Bacterial carboxyl-terminal processing proteases (CTPs) are critical for maintaining protein quality control, mediating signal transduction, and enabling cellular adaptation. Their activation typically involves substrate binding to the PDZ domain or interaction with an adaptor protein. In this study, we employed hydrogen–deuterium exchange mass spectrometry (HDX-MS) to investigate the conformational dynamics of the CTP from Helicobacter pylori, CtpA, in both the presence and absence of its substrate HP1076. To eliminate the confounding effects of proteolysis, a triple mutant (CtpATM) with an inactivated catalytic triad was used. Additionally, a hinge-region mutant (CtpAF105R) was employed to validate the dynamic behavior of the linker connecting the PDZ domain. This study reveals CtpA transitions between resting and active states independently of substrate binding.
HostingRepository	PRIDE
AnnounceDate	2025-10-04
AnnouncementXML	Submission_2025-10-04_03:48:58.589.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Kailei Sun
SpeciesList	scientific name: Helicobacter pylori G27; NCBI TaxID: NEWT:563041;
ModificationList	No PTMs are included in the dataset
Instrument	Synapt MS

Revision	Datetime	Status	ChangeLog Entry
0	2025-09-26 16:03:41	ID requested
⏵ 1	2025-10-04 03:48:59	announced

Dataset with its publication pending

submitter keyword: CtpA, protease, HDX-MS, Helicobacter pylori

Shannon Wing Ngor Au
contact affiliation	School of Life Sciences, The Chinese University of Hong Kong
contact email	shannon-au@cuhk.edu.hk
lab head
Kailei Sun
contact affiliation	The Chinese University of Hong Kong
contact email	kaileisun@cuhk.edu.hk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD068881
     1. Label: PRIDE project
     2. Name: Study of the conformational dynamics of Helicobacter pylori CtpA