1qcs: Difference between revisions
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'''N-TERMINAL DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)''' | '''N-TERMINAL DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)''' | ||
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[[Category: Jahn, R.]] | [[Category: Jahn, R.]] | ||
[[Category: Yu, R C.]] | [[Category: Yu, R C.]] | ||
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Revision as of 03:08, 3 May 2008
N-TERMINAL DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)
Overview
N-ethylmaleimide-sensitive factor (NSF) is a hexameric ATPase essential for eukaryotic vesicle fusion. Along with SNAP proteins, it disassembles cis-SNARE complexes upon ATP hydrolysis, preparing SNAREs for trans complex formation. We have determined the crystal structure of the N-terminal domain of NSF (N) to 1.9 A resolution. N contains two subdomains which form a groove that is a likely SNAP interaction site. Unexpectedly, both N subdomains are structurally similar to domains in EF-Tu. Based on this similarity, we propose a model for a large conformational change in NSF that drives SNARE complex disassembly.
About this Structure
1QCS is a Single protein structure of sequence from Cricetulus griseus. Full crystallographic information is available from OCA.
Reference
NSF N-terminal domain crystal structure: models of NSF function., Yu RC, Jahn R, Brunger AT, Mol Cell. 1999 Jul;4(1):97-107. PMID:10445031 Page seeded by OCA on Sat May 3 06:08:17 2008