5dje: Difference between revisions

Latest revision as of 21:43, 28 June 2023

Crystal structure of the zuotin homology domain (ZHD) from yeast Zuo1

Structural highlights

5dje is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:	BTB, EDO, MSE, PEG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ZUO1_YEAST Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1.^[1] ^[2]

Publication Abstract from PubMed

Ribosome-associated J protein-Hsp70 chaperones promote nascent-polypeptide folding and normal translational fidelity. The J protein Zuo1 is known to span the ribosomal subunits, but understanding of its function is limited. Here we present new structural and cross-linking data allowing more precise positioning of Saccharomyces cerevisiae Zuo1 near the 60S polypeptide-exit site and suggesting interactions of Zuo1 with the ribosomal protein eL31 and 25S rRNA helix 24. The junction between the 60S-interacting and subunit-spanning helices is a hinge that positions Zuo1 on the 40S yet accommodates subunit rotation. Interaction between the Zuo1 C terminus and 40S occurs via 18S rRNA expansion segment 12 (ES12) of helix 44, which originates at the decoding site. Deletions in either ES12 or the Zuo1 C terminus alter readthrough of stop codons and -1 frameshifting. Our study offers insight into how this cotranslational chaperone system may monitor decoding-site activity and nascent-polypeptide transit, thereby coordinating protein translation and folding.

Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits.,Lee K, Sharma R, Shrestha OK, Bingman CA, Craig EA Nat Struct Mol Biol. 2016 Sep 26. doi: 10.1038/nsmb.3299. PMID:27669034^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rakwalska M, Rospert S. The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae. Mol Cell Biol. 2004 Oct;24(20):9186-97. PMID:15456889 doi:https://dx.doi.org/10.1128/MCB.24.20.9186-9197.2004
↑ Huang P, Gautschi M, Walter W, Rospert S, Craig EA. The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol. 2005 Jun;12(6):497-504. Epub 2005 May 22. PMID:15908962 doi:https://dx.doi.org/10.1038/nsmb942
↑ Lee K, Sharma R, Shrestha OK, Bingman CA, Craig EA. Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits. Nat Struct Mol Biol. 2016 Sep 26. doi: 10.1038/nsmb.3299. PMID:27669034 doi:https://dx.doi.org/10.1038/nsmb.3299

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Rakwalska M, Rospert S. The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae. Mol Cell Biol. 2004 Oct;24(20):9186-97. PMID:15456889 doi:https://dx.doi.org/10.1128/MCB.24.20.9186-9197.2004

[2] Huang P, Gautschi M, Walter W, Rospert S, Craig EA. The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol. 2005 Jun;12(6):497-504. Epub 2005 May 22. PMID:15908962 doi:https://dx.doi.org/10.1038/nsmb942

[3] Lee K, Sharma R, Shrestha OK, Bingman CA, Craig EA. Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits. Nat Struct Mol Biol. 2016 Sep 26. doi: 10.1038/nsmb.3299. PMID:27669034 doi:https://dx.doi.org/10.1038/nsmb.3299

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='5dje' size='340' side='right'caption='[[5dje]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5dje]] is a 2 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=5DJE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DJE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5dje]] is a 2 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=5DJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DJE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZUO1, YGR285C ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5dje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dje OCA], [https://pdbe.org/5dje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dje RCSB], [https://www.ebi.ac.uk/pdbsum/5dje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dje ProSAT]</span></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=5dje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dje OCA], [http://pdbe.org/5dje PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dje RCSB], [http://www.ebi.ac.uk/pdbsum/5dje PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dje ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ZUO1_YEAST ZUO1_YEAST]] Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1.<ref>PMID:15456889</ref> <ref>PMID:15908962</ref>
+[https://www.uniprot.org/uniprot/ZUO1_YEAST ZUO1_YEAST] Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1.<ref>PMID:15456889</ref> <ref>PMID:15908962</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Baker's yeast]]
 [[Category: Large Structures]]
-[[Category: Bingman, C A]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Craig, E A]]
+[[Category: Bingman CA]]
-[[Category: Shrestha, O K]]
+[[Category: Craig EA]]
-[[Category: Chaperone]]
+[[Category: Shrestha OK]]
-[[Category: Hsp-40]]
-[[Category: J-protein]]
-[[Category: Molecular chaperone]]
-[[Category: Ribomsome association]]

5dje: Difference between revisions

Latest revision as of 21:43, 28 June 2023

Crystal structure of the zuotin homology domain (ZHD) from yeast Zuo1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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