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==Cryo-EM structure of native H. thermoluteolus TH-1 GroEL== | |||
<StructureSection load='8wu4' size='340' side='right'caption='[[8wu4]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8wu4]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydrogenophilus_thermoluteolus Hydrogenophilus thermoluteolus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WU4 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]] 3.3Å</td></tr> | |||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8wu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wu4 OCA], [https://pdbe.org/8wu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wu4 RCSB], [https://www.ebi.ac.uk/pdbsum/8wu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wu4 ProSAT]</span></td></tr> | ||
[[Category: Arakawa | </table> | ||
[[Category: Fushinobu | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/A0A2Z6DW38_HYDTE A0A2Z6DW38_HYDTE] Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.[HAMAP-Rule:MF_00600][RuleBase:RU000419] | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Hydrogenophilus thermoluteolus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arakawa T]] | ||
[[Category: Fushinobu S]] | |||
[[Category: Gerle C]] | |||
[[Category: Gopalasingam CC]] | |||
[[Category: Ishii M]] | |||
[[Category: Kameya M]] | |||
[[Category: Liao Z]] | |||
[[Category: Shigematsu H]] | |||
Latest revision as of 13:14, 27 March 2024
Cryo-EM structure of native H. thermoluteolus TH-1 GroELCryo-EM structure of native H. thermoluteolus TH-1 GroEL
Structural highlights
FunctionA0A2Z6DW38_HYDTE Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.[HAMAP-Rule:MF_00600][RuleBase:RU000419] |
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