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

Inokentijs Josts1, Christopher James Stubenrauch2, Grishma Vadlamani2

  • 1The 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.

Structure (London, England : 1993)
|November 14, 2017
PubMed

Insights

The translocation and assembly module (TAM) protein TamB

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • The translocation and assembly module (TAM) facilitates protein transport into the bacterial outer membrane.
  • TamB is a key component of the TAM system, but its structure and function remain poorly understood.

Purpose of the Study:

  • To elucidate the structure and potential mechanism of TamB, a crucial protein in bacterial outer membrane biogenesis.

Main Methods:

  • X-ray crystallography was used to determine the structure of a significant portion of TamB (amino acids 963-1,138).
  • Bioinformatic sequence analysis was performed to infer the broader structural characteristics of TamB.

Main Results:

  • The crystal structure of TamB963-1138 revealed a taco-shaped β-sheet with a hydrophobic interior.
  • This unique structure is capable of binding and shielding hydrophobic protein segments, suggesting a chaperone role.

Conclusions:

  • The identified β-taco structure of TamB likely enables it to chaperone nascent membrane proteins.
  • This structural insight provides a potential mechanism for TamB acting as a conduit in protein transport across the periplasmic space.
Keywords:
Escherichia coliTamBX-ray crystallographychaperonemembrane biologymicrobiologyprotein assembly

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