1QCS

N-TERMINAL DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)

Summary for 1QCS

• Entry DOI: 10.2210/pdb1qcs/pdb
• Related: 1d2n 1nsf
• Descriptor: N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF-N), SULFATE ION (3 entities in total)
• Functional Keywords: double-psi beta barrel alpha beta roll, fusion protein
• Biological source: Cricetulus griseus (Chinese hamster)
• Cellular location: Cytoplasm: P18708
• Total number of polymer chains: 1
• Total formula weight: 23837.14

Authors

Yu, R.C.,Jahn, R.,Brunger, A.T. (deposition date: 1999-05-14, release date: 1999-05-18, Last modification date: 2024-10-09)

Primary citation

Yu, R.C.,Jahn, R.,Brunger, A.T.
NSF N-terminal domain crystal structure: models of NSF function.
Mol.Cell, 4:97-107, 1999

PubMed Abstract: 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.

PubMed: 10445031
DOI: 10.1016/S1097-2765(00)80191-4

Experimental method

X-RAY DIFFRACTION (1.9 Å)