The structure of a conserved domain of TamB reveals a hydrophobic β taco fold

Josts, I., Stubenrauch, C. J., Vadlamani, G., Mosbahi, K., Walker, D. , Lithgow, T. and Grinter, R. (2017) The structure of a conserved domain of TamB reveals a hydrophobic β taco fold. Structure, 25(12), 1898-1906.e5. (doi:10.1016/j.str.2017.10.002) (PMID:29129383) (PMCID:PMC5719984)

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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.

Item Type:Articles
Keywords:Escherichia coli, TamB, X-ray crystallography, chaperone, membrane biology, microbiology, protein assembly.
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Walker, Professor Daniel and Mosbahi, Dr Khedidja
Authors: Josts, I., Stubenrauch, C. J., Vadlamani, G., Mosbahi, K., Walker, D., Lithgow, T., and Grinter, R.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Structure
Publisher:Elsevier
ISSN:0969-2126
ISSN (Online):1878-4186
Published Online:09 November 2017
Copyright Holders:Copyright © 2017 The Authors
First Published:First published in Structure 25(12(1898-1906.e5)
Publisher Policy:Reproduced under a Creative Commons License

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
558551Development of pyocins active against Pseudomonas aeruginosaDaniel WalkerWellcome Trust (WELLCOTR)093592/Z/10/ZIII - BACTERIOLOGY