PDBsum entry 4s0f

Transport protein/hydrolase

PDB id: 4s0f

Contents

Protein chains

565 a.a.

Ligands

AGS ×2

References listed in PDB file

Key reference

• Title: Crystal structures of a polypeptide processing and secretion transporter.
• Authors: D.Y.Lin, S.Huang, J.Chen.
• Ref.: Nature, 2015, 523, 425-430. [DOI no: 10.1038/nature14623]
• PubMed id: 26201595

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.