1NSF

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

Summary for 1NSF

• Entry DOI: 10.2210/pdb1nsf/pdb
• Descriptor: N-ETHYLMALEIMIDE SENSITIVE FACTOR, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: protein transport, endoplasmic reticulum, golgi stack, atp-binding
• Biological source: Cricetulus griseus (Chinese hamster)
• Cellular location: Cytoplasm: P18708
• Total number of polymer chains: 1
• Total formula weight: 31017.94

Authors

Yu, R.C.,Hanson, P.I.,Jahn, R.,Brunger, A.T. (deposition date: 1998-06-26, release date: 1998-11-25, Last modification date: 2024-02-14)

Primary citation

Yu, R.C.,Hanson, P.I.,Jahn, R.,Brunger, A.T.
Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP.
Nat.Struct.Biol., 5:803-811, 1998

PubMed Abstract: 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.

PubMed: 9731775
DOI: 10.1038/1843

Experimental method

X-RAY DIFFRACTION (1.9 Å)