4RY2

Crystal structure of the peptidase-containing ABC transporter PCAT1

Summary for 4RY2

• Entry DOI: 10.2210/pdb4ry2/pdb
• Related: 4S0F
• Descriptor: ABC-type bacteriocin transporter (1 entity in total)
• Functional Keywords: c39 peptidase, abc transporter, bacteriocin transporter, bi-functional abc transporter, atp-binding cassette transporters, atp binding, membrane, transport protein-hydrolase complex, transport protein/hydrolase
• Biological source: Ruminiclostridium thermocellum ATCC 27405
• Total number of polymer chains: 2
• Total formula weight: 162361.61

Authors

Lin, D.L.,Huang, S.,Chen, J. (deposition date: 2014-12-13, release date: 2015-07-22, Last modification date: 2023-09-20)

Primary citation

Lin, D.Y.,Huang, S.,Chen, J.
Crystal structures of a polypeptide processing and secretion transporter.
Nature, 523:425-430, 2015

PubMed 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.

PubMed: 26201595
DOI: 10.1038/nature14623

Experimental method

X-RAY DIFFRACTION (3.611 Å)