Crystal structures of a polypeptide processing and secretion transporter

International Conference on Applied Crystallography
October 16-17, 2017 | Chicago, USA

David Lin

Iowa State University, USA

Posters & Accepted Abstracts: Struct Chem Crystallogr Commun

DOI: 10.21767/2470-9905-C1-003

Abstract

Bacteria secrete peptides and proteins to communicate, to poison competitors, and to manipulate host cells. In Gram-positive bacteria, peptidase-containing ABC transporters (PCATs) function both as maturation proteases and as exporters for quorumsensing or antimicrobial polypeptides. In Gram-negative bacteria, PCATs interact with two other membrane proteins to form the type 1 secretion system. We showed here the first 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 �?±-helical barrel sufficient to accommodate small folded proteins. ATP binding alternates access to the transmembrane pathway and regulates the protease activity, thereby coupling substrate processing to translocation.

paper.io

agar io

wowcappadocia.com
cappadocia-hotels.com
caruscappadocia.com
brothersballoon.com
balloon-rides.net

wormax io