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1d2n
From Proteopedia
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| , resolution 1.75Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 30 19:33:21 2008
