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==Peptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegans== | ==Peptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegans== | ||
<StructureSection load='2op6' size='340' side='right' caption='[[2op6]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2op6' size='340' side='right'caption='[[2op6]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2op6]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2op6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OP6 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</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=2op6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2op6 OCA], [https://pdbe.org/2op6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2op6 RCSB], [https://www.ebi.ac.uk/pdbsum/2op6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2op6 ProSAT], [https://www.topsan.org/Proteins/MCSG/2op6 TOPSAN]</span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<table> | == Function == | ||
[https://www.uniprot.org/uniprot/BIBH_CAEEL BIBH_CAEEL] Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions (PubMed:15716356). Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion (PubMed:15716356).[UniProtKB:P11021]<ref>PMID:15716356</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/op/2op6_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/op/2op6_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=2op6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Heat Shock | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Duggan E]] | ||
[[Category: | [[Category: Gu M]] | ||
[[Category: | [[Category: Joachimiak A]] | ||
[[Category: Morimoto | [[Category: Morimoto RI]] | ||
[[Category: Osipiuk | [[Category: Osipiuk J]] | ||
[[Category: Voisine | [[Category: Voisine C]] | ||
Latest revision as of 13:46, 30 August 2023
Peptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegansPeptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegans
Structural highlights
FunctionBIBH_CAEEL Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions (PubMed:15716356). Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion (PubMed:15716356).[UniProtKB:P11021][1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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