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[[Image:2o1u.jpg|left|200px]]<br /><applet load="2o1u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2o1u, resolution 2.40&Aring;" />
'''Structure of full length GRP94 with AMP-PNP bound'''<br />


==Overview==
==Structure of full length GRP94 with AMP-PNP bound==
GRP94, an essential endoplasmic reticulum chaperone, is required for the conformational maturation of proteins destined for cell-surface display or export. The extent to which GRP94 and its cytosolic paralog, Hsp90, share a common mechanism remains controversial. GRP94 has not been shown conclusively to hydrolyze ATP or bind cochaperones, and both activities, by contrast, result in conformational changes and N-terminal dimerization in Hsp90 that are critical for its function. Here, we report the 2.4 A crystal structure of mammalian GRP94 in complex with AMPPNP and ADP. The chaperone is conformationally insensitive to the identity of the bound nucleotide, adopting a "twisted V" conformation that precludes N-terminal domain dimerization. We also present conclusive evidence that GRP94 possesses ATPase activity. Our observations provide a structural explanation for GRP94's observed rate of ATP hydrolysis and suggest a model for the role of ATP binding and hydrolysis in the GRP94 chaperone cycle.
<StructureSection load='2o1u' size='340' side='right'caption='[[2o1u]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2o1u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. The December 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hsp90''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_12 10.2210/rcsb_pdb/mom_2008_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O1U 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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2o1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1u OCA], [https://pdbe.org/2o1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o1u RCSB], [https://www.ebi.ac.uk/pdbsum/2o1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o1u 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/o1/2o1u_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=2o1u ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2O1U 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 <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O1U OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones., Dollins DE, Warren JJ, Immormino RM, Gewirth DT, Mol Cell. 2007 Oct 12;28(1):41-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17936703 17936703]
[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
[[Category: Single protein]]
[[Category: Hsp90]]
[[Category: Dollins, D E.]]
[[Category: Large Structures]]
[[Category: Gewirth, D T.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Immormino, R M.]]
[[Category: Dollins DE]]
[[Category: Warren, J J.]]
[[Category: Gewirth DT]]
[[Category: ANP]]
[[Category: Immormino RM]]
[[Category: MG]]
[[Category: Warren JJ]]
[[Category: amp-pnp]]
[[Category: chaperone]]
[[Category: endoplasmin]]
[[Category: gp96]]
[[Category: grp94]]
[[Category: hsp82]]
[[Category: hsp90]]
[[Category: htpg]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:13:31 2008''

Latest revision as of 09:28, 3 April 2024

Structure of full length GRP94 with AMP-PNP boundStructure of full length GRP94 with AMP-PNP bound

Structural highlights

2o1u is a 2 chain structure with sequence from Canis lupus familiaris. The December 2008 RCSB PDB Molecule of the Month feature on Hsp90 by David Goodsell is 10.2210/rcsb_pdb/mom_2008_12. 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

2o1u, resolution 2.40Å

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