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TitleStructural basis of substrate recognition by a polypeptide processing and secretion transporter.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateJan 14, 2020
AuthorsVirapat Kieuvongngam / Paul Dominic B Olinares / Anthony Palillo / Michael L Oldham / Brian T Chait / Jue Chen /
PubMed AbstractThe peptidase-containing ATP-binding cassette transporters (PCATs) are unique members of the ABC transporter family that proteolytically process and export peptides and proteins. Each PCAT contains ...The peptidase-containing ATP-binding cassette transporters (PCATs) are unique members of the ABC transporter family that proteolytically process and export peptides and proteins. Each PCAT contains two peptidase domains that cleave off the secretion signal, two transmembrane domains forming a translocation pathway, and two nucleotide-binding domains that hydrolyze ATP. Previously the crystal structures of a PCAT from (PCAT1) were determined in the absence and presence of ATP, revealing how ATP binding regulates the protease activity and access to the translocation pathway. However, how the substrate CtA, a 90-residue polypeptide, is recognized by PCAT1 remained elusive. To address this question, we determined the structure of the PCAT1-CtA complex by electron cryo-microscopy (cryo-EM) to 3.4 Å resolution. The structure shows that two CtAs are bound via their N-terminal leader peptides, but only one is positioned for cleavage and translocation. Based on these results, we propose a model of how substrate cleavage, ATP hydrolysis, and substrate translocation are coordinated in a transport cycle.
External linksElife / PubMed:31934861 / PubMed Central
MethodsEM (single particle)
Resolution3.35 Å
Structure data

21132

6v9z

EMDB-21132, PDB-6v9z:
Cryo-EM structure of PCAT1 bound to its CtA peptide substrate
Method: EM (single particle) / Resolution: 3.35 Å

Source
  • Hungateiclostridium thermocellum (bacteria)
  • hungateiclostridium thermocellum (strain atcc 27405 / dsm 1237 / jcm 9322 / nbrc 103400 / ncimb 10682 / nrrl b-4536 / vpi 7372) (bacteria)
KeywordsPROTEIN TRANSPORT / ATP-Binding Cassette

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