5VTG

The structure of TamB963-1138 from Escherichia coli reveals a novel hydrophobic Beta-taco fold

Summary for 5VTG

• Entry DOI: 10.2210/pdb5vtg/pdb
• Descriptor: Translocation and assembly module subunit TamB (2 entities in total)
• Functional Keywords: chaperone, beta-sheet, periplasm
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane ; Single-pass membrane protein : P39321
• Total number of polymer chains: 2
• Total formula weight: 40237.05

Authors

Grinter, R.,Josts, I. (deposition date: 2017-05-17, release date: 2017-11-22, Last modification date: 2024-03-13)

Primary citation

Josts, I.,Stubenrauch, C.J.,Vadlamani, G.,Mosbahi, K.,Walker, D.,Lithgow, T.,Grinter, R.
The Structure of a Conserved Domain of TamB Reveals a Hydrophobic beta Taco Fold.
Structure, 25:1898-1906.e5, 2017

PubMed 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. TamB 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 TamB is shared by a large portion of TamB. This architecture could allow TamB to act as a conduit for membrane proteins.

PubMed: 29129383
DOI: 10.1016/j.str.2017.10.002

Experimental method

X-RAY DIFFRACTION (1.859 Å)