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The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex
Daniel Kümmel1, Jürgen J Müller, Yvette Roske
1Max-Delbrück Center for Molecular Medicine, Berlin, Germany.
EMBO Reports
|July 19, 2005
Summary
The crystal structure of human TPC6, a transport protein particle (TRAPP) subunit, reveals structural similarity to BET3. This suggests heterodimerization, highlighting conserved structural roles in vesicle transport.
Area of Science:
- Cell biology
- Structural biology
- Protein structure and function
Background:
- Transport protein particle (TRAPP) complexes are crucial for vesicle transport.
- Previous studies determined crystal structures for TRAPP subunits SEDL and BET3.
Purpose of the Study:
- To determine the crystal structure of the human TRAPP subunit TPC6.
- To investigate the structural relationship between TPC6 and other TRAPP subunits, particularly BET3.
- To explore the potential heterodimerization of TPC6 and BET3.
Main Methods:
- X-ray crystallography to determine the 1.7 Angstroms crystal structure of human TPC6.
- In vitro and in vivo association studies to confirm protein interactions.
Main Results:
- The crystal structure of TPC6 was determined, revealing an alpha/beta-plait topology and dimer formation.
- TPC6 shares striking structural similarity with BET3, particularly at dimerization interfaces, despite low sequence similarity.
- Heterodimerization of TPC6 and BET3 was confirmed through association studies.
Conclusions:
- TPC6 and BET3 likely form heterodimers, suggesting a conserved functional role within TRAPP complexes.
- TPC6, BET3, and TPC5 may represent a family of paralogous proteins with similar 3D structures but divergent sequences.
- Structural insights into TPC6 contribute to understanding the molecular mechanisms of vesicle transport.