Dataset Information

Cleaved Ycf1p mass spectrometry analysis

ABSTRACT: LC MS/MS analysis of site of Pep4-mediated cleavage of Ycf1p

INSTRUMENT(S):

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Voula Kanelis

LAB HEAD: Voula Kanelis

PROVIDER: PXD057166 | Pride | 2025-05-07

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	20200120_UVPD_CDS_BickersS_ABC_core.mgf	Mgf
	20200120_UVPD_CDS_BickersS_ABC_core.raw	Raw
	20200120_UVPD_CDS_BickersS_TMDO.mgf	Mgf
	20200120_UVPD_CDS_BickersS_TMDO.raw	Raw
	ABCcore_peptides_1_1_0.mzid.gz	Mzid

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Publications

Structure of a dimeric full-length ABC transporter.

Bickers Sarah C SC Benlekbir Samir S Rubinstein John L JL Kanelis Voula V

Nature communications 20241116 1

Activities of ATP binding cassette (ABC) proteins are regulated by multiple mechanisms, including protein interactions, phosphorylation, proteolytic processing, and/or oligomerization of the ABC protein itself. Here we present the structure of yeast cadmium factor 1 (Ycf1p) in its mature form following cleavage by Pep4p protease. Ycf1p, a C subfamily ABC protein (ABCC), is homologue of human multidrug resistance protein 1. Remarkably, a portion of cleaved Ycf1p forms a well-ordered dimer, alongs ...[more]

PMID: 39550367

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