1d2n
From Proteopedia
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D2 DOMAIN OF N-ETHYLMALEIMIDE-SENSITIVE FUSION PROTEIN
Overview
N-ethylmaleimide-sensitive fusion protein (NSF) is a cytosolic ATPase, required for many intracellular vesicle fusion reactions. NSF consists of, an amino-terminal region that interacts with other components of the, vesicle trafficking machinery, followed by two homologous ATP-binding, cassettes, designated D1 and D2, that possess essential ATPase and, hexamerization activities, respectively. The crystal structure of D2 bound, to Mg2+-AMPPNP has been determined at 1.75 A resolution. The structure, consists of a nucleotide-binding and a helical domain, and it is, unexpectedly similar to the first two domains of the clamp-loading subunit, delta' of E. coli DNA polymerase III. The structure suggests several, regions responsible for coupling of ATP hydrolysis to structural changes, in full-length NSF.
About this Structure
1D2N is a Single protein structure of sequence from Cricetulus griseus with MG, ANP and GOL as ligands. The following page contains interesting information on the relation of 1D2N with [AAA+ Proteases]. Full crystallographic information is available from OCA.
Reference
Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein., Lenzen CU, Steinmann D, Whiteheart SW, Weis WI, Cell. 1998 Aug 21;94(4):525-36. PMID:9727495
Page seeded by OCA on Sun Nov 18 08:58:40 2007
Categories: AAA+ Proteases | Cricetulus griseus | Single protein | Lenzen, C.U. | Steinmann, D. | Weis, W.I. | Whiteheart, S.W. | ANP | GOL | MG | Atpase | Hexamerization domain | Transport
