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==Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS== | |||
<StructureSection load='6xlh' size='340' side='right'caption='[[6xlh]], [[Resolution|resolution]] 2.83Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6xlh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XLH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.83Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xlh OCA], [https://pdbe.org/6xlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xlh RCSB], [https://www.ebi.ac.uk/pdbsum/6xlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xlh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HSC82_YEAST HSC82_YEAST] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.<ref>PMID:11094077</ref> | |||
==See Also== | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Agard DA]] | |||
[[Category: Elnatan D]] | |||
[[Category: Liu YX]] | |||
[[Category: Myasnikov AG]] | |||
[[Category: Sun M]] | |||
Latest revision as of 17:50, 6 March 2024
Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaSAsymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS
Structural highlights
FunctionHSC82_YEAST Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.[1] See AlsoReferences
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