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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Rice LM,Brunger ATdoi
10.1016/s1097-2765(00)80190-2subject
Has Abstractpub_date
1999-07-01 00:00:00pages
85-95issue
1eissn
1097-2765issn
1097-4164pii
S1097-2765(00)80190-2journal_volume
4pub_type
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