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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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Yu RC, Hanson PI, Jahn R, Brunger AT. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat Struct Biol. 1998 Sep;5(9):803-11. PMID:9731775 doi:10.1038/1843
