1nsf

D2 HEXAMERIZATION DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)D2 HEXAMERIZATION DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)

Structural highlights 1nsf is a 1 chain structure with sequence from Cho cell lines. The August 2006 RCSB PDB Molecule of the Month feature on AAA+ Proteases by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_8. The November 2013 RCSB PDB Molecule of the Month feature on SNARE Proteins by David Goodsell is 10.2210/rcsb_pdb/mom_2013_11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [NSF_CRIGR] Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seem to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed N-ethylmaleimide-sensitive factor (NSF) is a hexameric ATPase which primes and/or dissociates SNARE complexes involved in intracellular fusion events. Each NSF protomer contains three domains: an N-terminal domain required for SNARE binding and two ATPase domains, termed D1 and D2, with D2 being required for oligomerization. We have determined the 1.9 A crystal structure of the D2 domain of NSF complexed with ATP using multi-wavelength anomalous dispersion phasing. D2 consists of a nucleotide binding subdomain with a Rossmann fold and a C-terminal subdomain, which is structurally unique among nucleotide binding proteins. There are interactions between the ATP moiety and both the neighboring D2 protomer and the C-terminal subdomain that may be important for ATP-dependent oligomerization. Of particular importance are three well-ordered and conserved lysine residues that form ionic interactions with the beta- and gamma-phosphates, one of which likely contributes to the low hydrolytic activity of D2. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP.,Yu RC, Hanson PI, Jahn R, Brunger AT Nat Struct Biol. 1998 Sep;5(9):803-11. PMID:9731775 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1nsf, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image