Article Metrics


Online attention

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

DOI: 10.1016/j.str.2017.10.002 DOI Help

Authors: Inokentijs Josts (University of Hamburg) , Christopher James Stubenrauch (Monash University) , Grishma Vadlamani (Monash University) , Khedidja Mosbahi (University of Glasgow) , Daniel Walker (University of Glasgow) , Trevor Lithgow (Monash University) , Rhys Grinter (Monash University; University of Birmingham)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure

State: Published (Approved)
Published: November 2017
Diamond Proposal Number(s): 6638 , 8659

Open Access Open Access

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.

Journal Keywords: Escherichia coli; TamB; microbiology; chaperone; membrane biology; protein assembly; X-ray crystallography

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography