1qdn: Difference between revisions

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New page: left|200px<br /><applet load="1qdn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qdn, resolution 2.30Å" /> '''AMINO TERMINAL DOMAI...
 
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'''AMINO TERMINAL DOMAIN OF THE N-ETHYLMALEIMIDE SENSITIVE FUSION PROTEIN (NSF)'''<br />


==Overview==
==AMINO TERMINAL DOMAIN OF THE N-ETHYLMALEIMIDE SENSITIVE FUSION PROTEIN (NSF)==
The cytosolic ATPase N-ethylmaleimide-sensitive fusion protein (NSF), disassembles complexes of membrane-bound proteins known as SNAREs, an, activity essential for vesicular trafficking. The amino-terminal domain of, NSF (NSF-N) is required for the interaction of NSF with the SNARE complex, through the adaptor protein alpha-SNAP. The crystal structure of NSF-N, reveals two subdomains linked by a single stretch of polypeptide. A polar, interface between the two subdomains indicates that they can move with, respect to one another during the catalytic cycle of NSF. Structure-based, sequence alignments indicate that in addition to NSF orthologues, the p97, family of ATPases contain an amino-terminal domain of similar structure.
<StructureSection load='1qdn' size='340' side='right'caption='[[1qdn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1qdn]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QDN FirstGlance]. <br>
1QDN 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 SO4 and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QDN OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qdn OCA], [https://pdbe.org/1qdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qdn RCSB], [https://www.ebi.ac.uk/pdbsum/1qdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qdn ProSAT]</span></td></tr>
Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein., May AP, Misura KM, Whiteheart SW, Weis WI, Nat Cell Biol. 1999 Jul;1(3):175-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10559905 10559905]
</table>
== Function ==
[https://www.uniprot.org/uniprot/NSF_CRIGR NSF_CRIGR] Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seem to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qd/1qdn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qdn ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Cricetulus griseus]]
[[Category: Cricetulus griseus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: May, A.P.]]
[[Category: May AP]]
[[Category: Misura, K.M.S.]]
[[Category: Misura KMS]]
[[Category: Weis, W.I.]]
[[Category: Weis WI]]
[[Category: Whiteheart, S.W.]]
[[Category: Whiteheart SW]]
[[Category: BME]]
[[Category: SO4]]
[[Category: double-psi beta barrel alpha/beta barrel]]
[[Category: vesicular-fusion protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:36:07 2007''

Latest revision as of 09:03, 17 April 2024

AMINO TERMINAL DOMAIN OF THE N-ETHYLMALEIMIDE SENSITIVE FUSION PROTEIN (NSF)AMINO TERMINAL DOMAIN OF THE N-ETHYLMALEIMIDE SENSITIVE FUSION PROTEIN (NSF)

Structural highlights

1qdn is a 3 chain structure with sequence from Cricetulus griseus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NSF_CRIGR Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seem to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1qdn, resolution 2.30Å

Drag the structure with the mouse to rotate

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OCA
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