6hb2: Difference between revisions
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New page: '''Unreleased structure''' The entry 6hb2 is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Structure of Hgh1, crystal form I, Selenomethionine derivative== | ||
<StructureSection load='6hb2' size='340' side='right'caption='[[6hb2]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6hb2]] 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=6HB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HB2 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6hb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hb2 OCA], [http://pdbe.org/6hb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hb2 RCSB], [http://www.ebi.ac.uk/pdbsum/6hb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hb2 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 6hb2" 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]] | |||
Latest revision as of 07:03, 27 March 2019
Structure of Hgh1, crystal form I, Selenomethionine derivative
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