1d2n: Difference between revisions
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|PDB= 1d2n |SIZE=350|CAPTION= <scene name='initialview01'>1d2n</scene>, resolution 1.75Å | |PDB= 1d2n |SIZE=350|CAPTION= <scene name='initialview01'>1d2n</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d2n OCA], [http://www.ebi.ac.uk/pdbsum/1d2n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d2n RCSB]</span> | |||
}} | }} | ||
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[[Category: Weis, W I.]] | [[Category: Weis, W I.]] | ||
[[Category: Whiteheart, S W.]] | [[Category: Whiteheart, S W.]] | ||
[[Category: atpase]] | [[Category: atpase]] | ||
[[Category: hexamerization domain]] | [[Category: hexamerization domain]] | ||
[[Category: transport]] | [[Category: transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:33:21 2008'' |
Revision as of 19:33, 30 March 2008
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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
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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
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