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Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex
1Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA.
Molecular Cell
|August 13, 1999
Summary
The crystal structure of yeast Sec17 (alpha-SNAP homolog) reveals its molecular architecture. This finding aids in understanding how SNAP proteins facilitate membrane trafficking by interacting with SNAREs and NSF.
Area of Science:
- Cell Biology
- Structural Biology
- Molecular Biology
Background:
- Soluble NSF Attachment Protein (SNAP) proteins are crucial for membrane trafficking in eukaryotic cells.
- SNAPs act as adaptors, linking SNARE proteins to the NSF chaperone for activation and recycling.
Purpose of the Study:
- To determine the high-resolution crystal structure of Sec17, the yeast homolog of alpha-SNAP.
- To elucidate the structural basis of SNAP protein function in membrane fusion.
Main Methods:
- X-ray crystallography was employed to determine the structure of Sec17.
- The structure was resolved to 2.9 Angstrom resolution.
Main Results:
- The crystal structure of Sec17 revealed a unique architecture comprising an N-terminal twisted sheet of alpha-helical hairpins and a C-terminal alpha-helical bundle.
- Local structural similarities were observed between Sec17's N-terminal sheet and tetratricopeptide repeats, though with a distinct twist.
- Sec17 shares structural features with HEAT and clathrin heavy chain repeats.
Conclusions:
- The determined structure provides insights into the molecular organization of SNAP proteins.
- Understanding Sec17's structure supports models where SNAPs act as lever arms in the NSF-mediated disassembly of SNARE complexes.
- This research contributes to the understanding of the fundamental mechanisms of membrane trafficking.