1qqe
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(New page: 200px<br /><applet load="1qqe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqe, resolution 2.90Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 22:46, 20 November 2007
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CRYSTAL STRUCTURE OF THE VESICULAR TRANSPORT PROTEIN SEC17
Overview
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.
About this Structure
1QQE is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly., Rice LM, Brunger AT, Mol Cell. 1999 Jul;4(1):85-95. PMID:10445030
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