2op6: Difference between revisions

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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]] 1.85&Aring;' scene=''>
<StructureSection load='2op6' size='340' side='right'caption='[[2op6]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2op6]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OP6 FirstGlance]. <br>
<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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yuw|1yuw]], [[1dky|1dky]], [[7hsc|7hsc]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hsp-4, hsp70d ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])</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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2op6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2op6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2op6 RCSB], [http://www.ebi.ac.uk/pdbsum/2op6 PDBsum], [http://www.topsan.org/Proteins/MCSG/2op6 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HSP7D_CAEEL HSP7D_CAEEL]] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER (By similarity).  
[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/chain_selection.php?pdb_ID=2ata ConSurf].
</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 Proteins|Heat Shock Proteins]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Duggan, E]]
[[Category: Large Structures]]
[[Category: Gu, M]]
[[Category: Duggan E]]
[[Category: Joachimiak, A]]
[[Category: Gu M]]
[[Category: Structural genomic]]
[[Category: Joachimiak A]]
[[Category: Morimoto, R I]]
[[Category: Morimoto RI]]
[[Category: Osipiuk, J]]
[[Category: Osipiuk J]]
[[Category: Voisine, C]]
[[Category: Voisine C]]
[[Category: Apc90014 13]]
[[Category: Hsp70/peptide-binding domain]]
[[Category: Mcsg]]
[[Category: Peptide binding protein]]
[[Category: PSI, Protein structure initiative]]

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