4S0F

Crystal structure of the peptidase-containing ABC transporter PCAT1 E648Q mutant complexed with ATPgS in an occluded conformation

4S0F の概要

• エントリーDOI: 10.2210/pdb4s0f/pdb
• 関連するPDBエントリー: 4RY2
• 分子名称: ABC-type bacteriocin transporter, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER (2 entities in total)
• 機能のキーワード: c39 peptidase, abc transporter, bacteriocin transporter, bi-functional abc transporter, atp-binding cassette transporters, membrane, transport protein-hydrolase complex, transport protein/hydrolase
• 由来する生物種: Ruminiclostridium thermocellum ATCC 27405
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 163406.12

構造登録者

Lin, D.L.,Huang, S.,Chen, J. (登録日: 2014-12-30, 公開日: 2015-07-22, 最終更新日: 2023-09-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (5.515 Å)