6hb1
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Hgh1, crystal form I== | |
| + | <StructureSection load='6hb1' size='340' side='right'caption='[[6hb1]], [[Resolution|resolution]] 2.33Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6hb1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HB1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HGH1, YGR187C, G7538 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=6hb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hb1 OCA], [http://pdbe.org/6hb1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hb1 RCSB], [http://www.ebi.ac.uk/pdbsum/6hb1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hb1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Eukaryotic elongation factor 2 (eEF2) is an abundant and essential component of the translation machinery. The biogenesis of this 93 kDa multi-domain protein is assisted by the chaperonin TRiC/CCT. Here, we show in yeast cells that the highly conserved protein Hgh1 (FAM203 in humans) is a chaperone that cooperates with TRiC in eEF2 folding. In the absence of Hgh1, a substantial fraction of newly synthesized eEF2 is degraded or aggregates. We solved the crystal structure of Hgh1 and analyzed the interaction of wild-type and mutant Hgh1 with eEF2. These experiments revealed that Hgh1 is an armadillo repeat protein that binds to the dynamic central domain III of eEF2 via a bipartite interface. Hgh1 binding recruits TRiC to the C-terminal eEF2 module and prevents unproductive interactions of domain III, allowing efficient folding of the N-terminal GTPase module. eEF2 folding is completed upon dissociation of TRiC and Hgh1. | ||
| - | + | Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2.,Monkemeyer L, Klaips CL, Balchin D, Korner R, Hartl FU, Bracher A Mol Cell. 2019 Mar 6. pii: S1097-2765(19)30054-1. doi:, 10.1016/j.molcel.2019.01.034. PMID:30876804<ref>PMID:30876804</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6hb1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Baker's yeast]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Balchin, D]] | ||
| + | [[Category: Bracher, A]] | ||
| + | [[Category: Hartl, F U]] | ||
| + | [[Category: Klaips, C L]] | ||
| + | [[Category: Koerner, R]] | ||
| + | [[Category: Moenkemeyer, L]] | ||
| + | [[Category: Armadillo repeat]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Solenoid protein]] | ||
Current revision
Structure of Hgh1, crystal form I
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