1yt0: Difference between revisions

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New page: left|200px<br /><applet load="1yt0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yt0, resolution 2.40Å" /> '''Crystal Structure of...
 
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[[Image:1yt0.jpg|left|200px]]<br /><applet load="1yt0" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH ADP'''<br />


==Overview==
==Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH ADP==
GRP94, the endoplasmic reticulum paralog of Hsp90, is regulated by, adenosine nucleotides that bind to its N-terminal regulatory domain., Because of its weak affinity for nucleotides, the functionally relevant, transition in GRP94 is likely to be between the unliganded and, nucleotide-bound states. We have determined the structure of the, unliganded GRP94 N-domain. The helix 1-4-5 subdomain of the unliganded, protein adopts the closed conformation seen in the structure of the, protein in complex with inhibitors. This conformation is distinct from the, open conformation of the subdomain seen when the protein is bound to ATP, or ADP. ADP soaked into crystals of the unliganded protein reveals an, intermediate conformation midway between the open and closed states and, demonstrates that in GRP94 the conversion between the open and closed, states is driven by ligand binding. The direction of the observed movement, in GRP94 shows that nucleotides act to open the subdomain elements rather, than close them, which is contrary to the motion proposed for Hsp90. These, observations support a model where ATP binding dictates the conformation, of the N-domain and regulates its ability to form quaternary structural, interactions.
<StructureSection load='1yt0' size='340' side='right'caption='[[1yt0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yt0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YT0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yt0 OCA], [https://pdbe.org/1yt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yt0 RCSB], [https://www.ebi.ac.uk/pdbsum/1yt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yt0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ENPL_CANLF ENPL_CANLF] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).
== 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/yt/1yt0_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=1yt0 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1YT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] with MG, ADP and PG4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YT0 OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change., Dollins DE, Immormino RM, Gewirth DT, J Biol Chem. 2005 Aug 26;280(34):30438-47. Epub 2005 Jun 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15951571 15951571]
[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dollins, D.E.]]
[[Category: Dollins DE]]
[[Category: Gewirth, D.T.]]
[[Category: Gewirth DT]]
[[Category: Immormino, R.M.]]
[[Category: Immormino RM]]
[[Category: ADP]]
[[Category: MG]]
[[Category: PG4]]
[[Category: adp]]
[[Category: atp]]
[[Category: bergerat]]
[[Category: chaperone]]
[[Category: endoplasmic reticulum]]
[[Category: gp96]]
[[Category: grp94]]
[[Category: hsp90]]
[[Category: htpg]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:02:05 2007''

Latest revision as of 11:59, 14 February 2024

Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH ADPCrystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH ADP

Structural highlights

1yt0 is a 1 chain structure with sequence from Canis lupus familiaris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENPL_CANLF Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).

Evolutionary Conservation

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

See Also

1yt0, resolution 2.40Å

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