Journal article
The Structure of a Conserved Domain of TamB Reveals a Hydrophobic β Taco Fold
I Josts, CJ Stubenrauch, G Vadlamani, K Mosbahi, D Walker, T Lithgow, R Grinter
Structure | Published : 2017
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 amphipa..
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Grants
Awarded by National Health and Medical Research Council
Funding Acknowledgements
Wethank the Diamond Light Source for access to beamlines I02, I04- 1, and I24 (proposal numbers MX6638 and MX8659). The work was funded by the NHMRC Program in Cellular Microbiology (1092262). R.G. was funded by a Sir Henry Wellcome Fellowship (award number 106077/Z/14/Z). During this work I.J. was supported by a studentship from the Wellcome Trust (award number 093592/Z/10/Z).