PDBsum entry 4s0f

Transport protein/hydrolase

PDB id: 4s0f

Contents

Protein chains

565 a.a.

Ligands

AGS ×2

PDB id:

4s0f

Name:

Transport protein/hydrolase

Title:

Crystal structure of the peptidase-containing abc transporter pcat1 e648q mutant complexed with atpgs in an occluded conformation

Structure:

Abc-type bacteriocin transporter. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Ruminiclostridium thermocellum atcc 27405. Organism_taxid: 203119. Strain: atcc 27405. Gene: abn51770.1, cthe_0534. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

5.52Å R-factor: 0.301 R-free: 0.314

Authors:

D.L.Lin,S.Huang,J.Chen

Key ref:

D.Y.Lin et al. (2015). Crystal structures of a polypeptide processing and secretion transporter. Nature, 523, 425-430. PubMed id: 26201595 DOI: 10.1038/nature14623

Date:

30-Dec-14 Release date: 22-Jul-15

Protein chains

A3DCU1  (A3DCU1_CLOTH) -  ABC-type bacteriocin transporter from Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)

Seq: 727 a.a.

Struc: 565 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.4.22.- - ?????

DOI no: 10.1038/nature14623

Nature 523:425-430 (2015)

PubMed id: 26201595

Crystal structures of a polypeptide processing and secretion transporter.

D.Y.Lin, S.Huang, J.Chen.

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.