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4ani
From Proteopedia
(Difference between revisions)
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<StructureSection load='4ani' size='340' side='right'caption='[[4ani]], [[Resolution|resolution]] 4.09Å' scene=''> | <StructureSection load='4ani' size='340' side='right'caption='[[4ani]], [[Resolution|resolution]] 4.09Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4ani]] is a 8 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4ani]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Geoka Geoka]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ANI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ANI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v7y|2v7y]]</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;'>[[2v7y|2v7y]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ani FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ani OCA], [https://pdbe.org/4ani PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ani RCSB], [https://www.ebi.ac.uk/pdbsum/4ani PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ani ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/GRPE_GEOKA GRPE_GEOKA]] Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding (By similarity). [[https://www.uniprot.org/uniprot/DNAK_GEOKA DNAK_GEOKA]] Acts as a chaperone (By similarity). |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
| - | *[[Heat Shock | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Geoka]] | [[Category: Geoka]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Chang, Y W]] | [[Category: Chang, Y W]] | ||
[[Category: Chien, C H]] | [[Category: Chien, C H]] | ||
Revision as of 05:40, 25 August 2022
Structural basis for the intermolecular communication between DnaK and GrpE in the DnaK chaperone system from Geobacillus kaustophilus HTA426
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