1nsf
|
D2 HEXAMERIZATION DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)
OverviewOverview
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.
About this StructureAbout this Structure
1NSF is a Single protein structure of sequence from Cricetulus griseus with MG and ATP as ligands. The following page contains interesting information on the relation of 1NSF with [AAA+ Proteases]. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Sun Nov 18 09:04:21 2007