6qt8: Difference between revisions
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The | ==Crystal structure of Rea1-MIDAS domain from Chaetomium thermophilum== | ||
<StructureSection load='6qt8' size='340' side='right'caption='[[6qt8]], [[Resolution|resolution]] 2.33Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6qt8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QT8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qta|6qta]], [[6qtb|6qtb]]</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=6qt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qt8 OCA], [http://pdbe.org/6qt8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qt8 RCSB], [http://www.ebi.ac.uk/pdbsum/6qt8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qt8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/G0SHE6_CHATD G0SHE6_CHATD]] Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits.[PIRNR:PIRNR010340] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Rea1 AAA(+)-ATPase dislodges assembly factors from pre-60S ribosomes upon ATP hydrolysis, thereby driving ribosome biogenesis. Here, we present crystal structures of Rea1-MIDAS, the conserved domain at the tip of the flexible Rea1 tail, alone and in complex with its substrate ligands, the UBL domains of Rsa4 or Ytm1. These complexes have structural similarity to integrin alpha-subunit domains when bound to extracellular matrix ligands, which for integrin biology is a key determinant for force-bearing cell-cell adhesion. However, the presence of additional motifs equips Rea1-MIDAS for its tasks in ribosome maturation. One loop insert cofunctions as an NLS and to activate the mechanochemical Rea1 cycle, whereas an additional beta-hairpin provides an anchor to hold the ligand UBL domains in place. Our data show the versatility of the MIDAS fold for mechanical force transmission in processes as varied as integrin-mediated cell adhesion and mechanochemical removal of assembly factors from pre-ribosomes. | |||
Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin-ligand-type complexes.,Ahmed YL, Thoms M, Mitterer V, Sinning I, Hurt E Nat Commun. 2019 Jul 11;10(1):3050. doi: 10.1038/s41467-019-10922-6. PMID:31296859<ref>PMID:31296859</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6qt8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ahmed, Y L]] | |||
[[Category: Hurt, E]] | |||
[[Category: Sinning, I]] | |||
[[Category: Thoms, M]] | |||
[[Category: Integrin]] | |||
[[Category: Mida]] | |||
[[Category: Ribosome]] | |||
[[Category: Ribosome biogenesis]] | |||
Latest revision as of 09:02, 7 August 2019
Crystal structure of Rea1-MIDAS domain from Chaetomium thermophilumCrystal structure of Rea1-MIDAS domain from Chaetomium thermophilum
Structural highlights
Function[G0SHE6_CHATD] Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits.[PIRNR:PIRNR010340] Publication Abstract from PubMedThe Rea1 AAA(+)-ATPase dislodges assembly factors from pre-60S ribosomes upon ATP hydrolysis, thereby driving ribosome biogenesis. Here, we present crystal structures of Rea1-MIDAS, the conserved domain at the tip of the flexible Rea1 tail, alone and in complex with its substrate ligands, the UBL domains of Rsa4 or Ytm1. These complexes have structural similarity to integrin alpha-subunit domains when bound to extracellular matrix ligands, which for integrin biology is a key determinant for force-bearing cell-cell adhesion. However, the presence of additional motifs equips Rea1-MIDAS for its tasks in ribosome maturation. One loop insert cofunctions as an NLS and to activate the mechanochemical Rea1 cycle, whereas an additional beta-hairpin provides an anchor to hold the ligand UBL domains in place. Our data show the versatility of the MIDAS fold for mechanical force transmission in processes as varied as integrin-mediated cell adhesion and mechanochemical removal of assembly factors from pre-ribosomes. Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin-ligand-type complexes.,Ahmed YL, Thoms M, Mitterer V, Sinning I, Hurt E Nat Commun. 2019 Jul 11;10(1):3050. doi: 10.1038/s41467-019-10922-6. PMID:31296859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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