1tc0

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[[Image:1tc0.gif|left|200px]]
 
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{{Structure
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==Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP==
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|PDB= 1tc0 |SIZE=350|CAPTION= <scene name='initialview01'>1tc0</scene>, resolution 2.20&Aring;
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<StructureSection load='1tc0' size='340' side='right'caption='[[1tc0]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>
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<table><tr><td colspan='2'>[[1tc0]] is a 2 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=1TC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TC0 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE= TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc0 OCA], [https://pdbe.org/1tc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1tc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tc0 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1qy5|1QY5]], [[1qy8|1QY8]], [[1qye|1QYE]], [[1qyh|1QYH]], [[1tbw|1TBW]], [[1tc6|1TC6]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc0 OCA], [http://www.ebi.ac.uk/pdbsum/1tc0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tc0 RCSB]</span>
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== Function ==
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}}
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tc/1tc0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1tc0 ConSurf].
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<div style="clear:both"></div>
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'''Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP'''
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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__TOC__
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==Overview==
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</StructureSection>
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GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with the N-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleotide-bound form exposes new surfaces that interact to form a biochemically plausible dimer that is reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP binding and a conformational change in response to ligand identity are distinctive mechanistic features of GRP94 and suggest a model for how GRP94 functions in the absence of co-chaperones and ATP hydrolysis.
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==About this Structure==
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1TC0 is a [[Single protein]] structure of sequence from [http://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=1TC0 OCA].
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==Reference==
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Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone., Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT, J Biol Chem. 2004 Oct 29;279(44):46162-71. Epub 2004 Aug 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15292259 15292259]
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[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dollins, D E.]]
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[[Category: Dollins DE]]
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[[Category: Gewirth, D T.]]
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[[Category: Gewirth DT]]
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[[Category: Immormino, R M.]]
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[[Category: Immormino RM]]
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[[Category: Shaffer, P L.]]
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[[Category: Shaffer PL]]
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[[Category: Soldano, K L.]]
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[[Category: Soldano KL]]
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[[Category: Walker, M A.]]
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[[Category: Walker MA]]
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[[Category: atp]]
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[[Category: bergerat]]
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[[Category: chaperone]]
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[[Category: endoplasmic reticulum]]
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[[Category: grp94]]
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[[Category: hsp90]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:54:03 2008''
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Current revision

Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP

PDB ID 1tc0

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