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E2 interaction and dimerization in the crystal structure of TRAF6.

Qian Yin¹, Su-Chang Lin, Betty Lamothe

¹Weill Medical College of Cornell University, New York, New York, USA.

Nature Structural & Molecular Biology

|May 26, 2009

Summary

Tumor necrosis factor (TNF) receptor-associated factor (TRAF)-6

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Area of Science:

Molecular Biology
Structural Biology
Immunology

Background:

Tumor necrosis factor (TNF) receptor-associated factor (TRAF)-6 is essential for NF-kappaB activation.
TRAF6 utilizes its N-terminal RING and zinc finger domains for mediating Lys63-linked polyubiquitination.

Purpose of the Study:

To elucidate the structural basis of TRAF6 function in polyubiquitination.
To investigate the role of TRAF6's N-terminal domains in its interaction with Ubc13 and its oligomeric state.

Main Methods:

X-ray crystallography to determine the structures of TRAF6 and its complex with Ubc13.
Structure-based mutagenesis to assess the functional importance of TRAF6 dimerization.
Fluorescence resonance energy transfer (FRET) to analyze higher-order oligomerization.

Main Results:

The crystal structures reveal a rigid, elongated conformation of TRAF6's RING and zinc finger domains.
TRAF6's N-terminal region forms a dimer in crystal and solution, which is critical for polyubiquitin synthesis and autoubiquitination.
TRAF6 dimerization promotes higher-order oligomerization of the full-length protein.

Conclusions:

TRAF6 dimerization, mediated by its N-terminal domains, is essential for its enzymatic activity in polyubiquitination.
The distinct dimeric and trimeric symmetries of TRAF6 may enable extensive oligomerization for immune receptor signaling.