Crystal structures of a polypeptide processing and secretion transporter

David Yin-wei Lin, Shuo Huang and Jue Chen ()
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David Yin-wei Lin: Laboratory of Membrane Biology and Biophysics, The Rockefeller University
Shuo Huang: Howard Hughes Medical Institute
Jue Chen: Laboratory of Membrane Biology and Biophysics, The Rockefeller University

Nature, 2015, vol. 523, issue 7561, 425-430

Abstract: Abstract Bacteria secrete peptides and proteins to communicate, to poison competitors, and to manipulate host cells. Among the various protein-translocation machineries, the peptidase-containing ATP-binding cassette transporters (PCATs) are appealingly simple. Each PCAT contains two peptidase domains that cleave the secretion signal from the substrate, two transmembrane domains that form a translocation pathway, and two nucleotide-binding domains that hydrolyse ATP. In Gram-positive bacteria, PCATs function both as maturation proteases and exporters for quorum-sensing or antimicrobial polypeptides. In Gram-negative bacteria, PCATs interact with two other membrane proteins to form the type 1 secretion system. Here we present crystal structures of PCAT1 from Clostridium thermocellum in two different conformations. These structures, accompanied by biochemical data, show that the translocation pathway is a large α-helical barrel sufficient to accommodate small folded proteins. ATP binding alternates access to the transmembrane pathway and also regulates the protease activity, thereby coupling substrate processing to translocation.

Date: 2015
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DOI: 10.1038/nature14623

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