Dataset Information

Investigating the dynamics of the SecA–SecYEG complex dynamic by HDX-MS

ABSTRACT: We employ hydrogen-deuterium exchange mass spectrometry (HDX-MS) to investigate the conformational dynamics required to facilitate based Brownian ratchet mechanism for protein secretion (by the SecA-SecYEG complex).

INSTRUMENT(S): Synapt MS

ORGANISM(S): Escherichia Coli

SUBMITTER: Zainab Ahdash

LAB HEAD: Argyris Politis

PROVIDER: PXD013594 | Pride | 2019-07-16

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	011118_SecA_YEG_ref_1_IA_final_peptide.csv	Csv
	011118_SecA_YEG_ref_2_IA_final_peptide.csv	Csv
	011118_SecA_YEG_ref_3_IA_final_peptide.csv	Csv
	291018_SecA_REF_1_IA_final_peptide.csv	Csv
	291018_SecA_REF_2_IA_final_peptide.csv	Csv

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Publications

HDX-MS reveals nucleotide-dependent, anti-correlated opening and closure of SecA and SecY channels of the bacterial translocon.

Ahdash Zainab Z Pyle Euan E Allen William John WJ Corey Robin A RA Collinson Ian I Politis Argyris A

eLife 20190710

The bacterial Sec translocon is a multi-protein complex responsible for translocating diverse proteins across the plasma membrane. For post-translational protein translocation, the Sec-channel - SecYEG - associates with the motor protein SecA to mediate the ATP-dependent transport of pre-proteins across the membrane. Previously, a diffusional-based Brownian ratchet mechanism for protein secretion has been proposed; the structural dynamics required to facilitate this mechanism remain unknown. Her ...[more]

PMID: 31290743

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