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1nsf

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|PDB= 1nsf |SIZE=350|CAPTION= <scene name='initialview01'>1nsf</scene>, resolution 1.90&Aring;
|PDB= 1nsf |SIZE=350|CAPTION= <scene name='initialview01'>1nsf</scene>, resolution 1.90&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsf OCA], [http://www.ebi.ac.uk/pdbsum/1nsf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nsf RCSB]</span>
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[[Category: Jahn, R.]]
[[Category: Jahn, R.]]
[[Category: Yu, R C.]]
[[Category: Yu, R C.]]
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[[Category: ATP]]
 
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[[Category: MG]]
 
[[Category: atp-binding]]
[[Category: atp-binding]]
[[Category: endoplasmic reticulum]]
[[Category: endoplasmic reticulum]]
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[[Category: protein transport]]
[[Category: protein transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:56:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:34:50 2008''

Revision as of 19:34, 30 March 2008


PDB ID 1nsf

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



D2 HEXAMERIZATION DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)


Overview

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 Structure

1NSF is a Single protein structure of sequence from Cricetulus griseus. The following page contains interesting information on the relation of 1NSF with [AAA+ Proteases]. Full crystallographic information is available from OCA.

Reference

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

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