3h0x: Difference between revisions

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==Crystal structure of peptide-binding domain of Kar2 protein from Saccharomyces cerevisiae==
==Crystal structure of peptide-binding domain of Kar2 protein from Saccharomyces cerevisiae==
<StructureSection load='3h0x' size='340' side='right' caption='[[3h0x]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
<StructureSection load='3h0x' size='340' side='right'caption='[[3h0x]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3h0x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H0X FirstGlance]. <br>
<table><tr><td colspan='2'>[[3h0x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H0X FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yuw|1yuw]], [[2op6|2op6]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yuw|1yuw]], [[2op6|2op6]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRP78, J1248, KAR2, SSD1, YJL034W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRP78, J1248, KAR2, SSD1, YJL034W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3h0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h0x OCA], [http://pdbe.org/3h0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h0x RCSB], [http://www.ebi.ac.uk/pdbsum/3h0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h0x ProSAT], [http://www.topsan.org/Proteins/MCSG/3h0x TOPSAN]</span></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=3h0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h0x OCA], [https://pdbe.org/3h0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h0x RCSB], [https://www.ebi.ac.uk/pdbsum/3h0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h0x ProSAT], [https://www.topsan.org/Proteins/MCSG/3h0x TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GRP78_YEAST GRP78_YEAST]] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.<ref>PMID:16002399</ref>   
[[https://www.uniprot.org/uniprot/GRP78_YEAST GRP78_YEAST]] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.<ref>PMID:16002399</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/h0/3h0x_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/3h0x_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>
Line 25: Line 25:
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Bigelow, L]]
[[Category: Bigelow, L]]
[[Category: Craig, E A]]
[[Category: Craig, E A]]

Revision as of 11:00, 16 March 2022

Crystal structure of peptide-binding domain of Kar2 protein from Saccharomyces cerevisiaeCrystal structure of peptide-binding domain of Kar2 protein from Saccharomyces cerevisiae

Structural highlights

3h0x is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:GRP78, J1248, KAR2, SSD1, YJL034W (ATCC 18824)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[GRP78_YEAST] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.[1]

Evolutionary Conservation

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

References

  1. ↑ Kimura T, Hosoda Y, Sato Y, Kitamura Y, Ikeda T, Horibe T, Kikuchi M. Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities. J Biol Chem. 2005 Sep 9;280(36):31438-41. Epub 2005 Jul 7. PMID:16002399 doi:http://dx.doi.org/10.1074/jbc.M503377200

3h0x, resolution 1.92Å

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