1QQE

CRYSTAL STRUCTURE OF THE VESICULAR TRANSPORT PROTEIN SEC17

Summary for 1QQE

• Entry DOI: 10.2210/pdb1qqe/pdb
• Descriptor: VESICULAR TRANSPORT PROTEIN SEC17 (2 entities in total)
• Functional Keywords: helix-turn-helix tpr-like repeat, protein transport
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Membrane; Peripheral membrane protein: P32602
• Total number of polymer chains: 1
• Total formula weight: 32824.73

Authors

Rice, L.M.,Brunger, A.T. (deposition date: 1999-06-04, release date: 1999-09-08, Last modification date: 2024-02-14)

Primary citation

Rice, L.M.,Brunger, A.T.
Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly.
Mol.Cell, 4:85-95, 1999

PubMed Abstract: SNAP proteins play an essential role in membrane trafficking in eukaryotic cells. They activate and recycle SNARE proteins by serving as adaptors between SNAREs and the cytosolic chaperone NSF. We have determined the crystal structure of Sec17, the yeast homolog of alpha-SNAP, to 2.9 A resolution. Sec17 is composed of an N-terminal twisted sheet of alpha-helical hairpins and a C-terminal alpha-helical bundle. The N-terminal sheet has local similarity to the tetratricopeptide repeats from protein phosphatase 5 but has a different overall twist. Sec17 also shares structural features with HEAT and clathrin heavy chain repeats. Possible models of SNAP:SNARE binding suggest that SNAPs may function as lever arms, transmitting forces generated by conformational changes in NSF/Sec18 to drive disassembly of SNARE complexes.

PubMed: 10445030
DOI: 10.1016/S1097-2765(00)80190-2

Experimental method

X-RAY DIFFRACTION (2.9 Å)