1fio
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(New page: 200px<br /><applet load="1fio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fio, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 12:49, 20 November 2007
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CRYSTAL STRUCTURE OF YEAST T-SNARE PROTEIN SSO1
Overview
In the eukaryotic secretory and endocytic pathways, transport vesicles, shuttle cargo among intracellular organelles and to and from the plasma, membrane. Cargo delivery entails fusion of the transport vesicle with its, target, a process thought to be mediated by membrane bridging SNARE, protein complexes. Temporal and spatial control of intracellular, trafficking depends in part on regulating the assembly of these complexes., In vitro, SNARE assembly is inhibited by the closed conformation adopted, by the syntaxin family of SNAREs. To visualize this closed conformation, directly, the X-ray crystal structure of a yeast syntaxin, Sso1p, has been, determined and refined to 2.1 A resolution. Mutants designed to, destabilize the closed conformation exhibit accelerated rates of SNARE, assembly. Our results provide insight into the mechanism of SNARE assembly, and its intramolecular and intermolecular regulation.
About this Structure
1FIO is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly., Munson M, Chen X, Cocina AE, Schultz SM, Hughson FM, Nat Struct Biol. 2000 Oct;7(10):894-902. PMID:11017200
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