1nsf
From Proteopedia
(New page: 200px<br /> <applet load="1nsf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nsf, resolution 1.90Å" /> '''D2 HEXAMERIZATION D...) |
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| - | [[Image:1nsf.gif|left|200px]]<br /> | + | [[Image:1nsf.gif|left|200px]]<br /><applet load="1nsf" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1nsf" size=" | + | |
caption="1nsf, resolution 1.90Å" /> | caption="1nsf, resolution 1.90Å" /> | ||
'''D2 HEXAMERIZATION DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)'''<br /> | '''D2 HEXAMERIZATION DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | N-ethylmaleimide-sensitive factor (NSF) is a hexameric ATPase which primes | + | 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== | ==About this Structure== | ||
| - | 1NSF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1NSF with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb80_1.html AAA+ Proteases]]. Full crystallographic information is available from [http:// | + | 1NSF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1NSF with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb80_1.html AAA+ Proteases]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cricetulus griseus]] | [[Category: Cricetulus griseus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brunger, A | + | [[Category: Brunger, A T.]] |
| - | [[Category: Hanson, P | + | [[Category: Hanson, P I.]] |
[[Category: Jahn, R.]] | [[Category: Jahn, R.]] | ||
| - | [[Category: Yu, R | + | [[Category: Yu, R C.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: protein transport]] | [[Category: protein transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:29 2008'' |
Revision as of 12:09, 21 February 2008
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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 with and as ligands. 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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