Affordable Access

deepdyve-link
Publisher Website

The Structure of a Conserved Domain of TamB Reveals a Hydrophobic β Taco Fold.

Authors
  • Josts, Inokentijs1
  • Stubenrauch, Christopher James2
  • Vadlamani, Grishma2
  • Mosbahi, Khedidja3
  • Walker, Daniel3
  • Lithgow, Trevor2
  • Grinter, Rhys4
  • 1 The Hamburg Centre for Ultrafast Imaging (CUI), Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany; Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany. , (Germany)
  • 2 Infection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC 3804, Australia. , (Australia)
  • 3 Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.
  • 4 Infection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC 3804, Australia; Institute of Microbiology and Infection, School of Immunity and Infection, University of Birmingham, Birmingham B15 2TT, UK. Electronic address: [email protected] , (Australia)
Type
Published Article
Journal
Structure
Publisher
Elsevier
Publication Date
Dec 05, 2017
Volume
25
Issue
12
Identifiers
DOI: 10.1016/j.str.2017.10.002
PMID: 29129383
Source
Medline
Keywords
License
Unknown

Abstract

The translocation and assembly module (TAM) plays a role in the transport and insertion of proteins into the bacterial outer membrane. TamB, a component of this system spans the periplasmic space to engage with its partner protein TamA. Despite efforts to characterize the TAM, the structure and mechanism of action of TamB remained enigmatic. Here we present the crystal structure of TamB amino acids 963-1,138. This region represents half of the conserved DUF490 domain, the defining feature of TamB. TamB963-1138 consists of a concave, taco-shaped β sheet with a hydrophobic interior. This β taco structure is of dimensions capable of accommodating and shielding the hydrophobic side of an amphipathic β strand, potentially allowing TamB to chaperone nascent membrane proteins from the aqueous environment. In addition, sequence analysis suggests that the structure of TamB963-1138 is shared by a large portion of TamB. This architecture could allow TamB to act as a conduit for membrane proteins.

Report this publication

Statistics

Seen <100 times