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1yjo

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Revision as of 07:14, 9 August 2023

Structure of NNQQNY from yeast prion Sup35 with zinc acetate

Structural highlights

1yjo is a 1 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 1.3Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ERF3_YEAST Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and amyloid-like fibrils can be formed in vitro. For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian prions. A seven-residue peptide segment from Sup35 forms amyloid-like fibrils and closely related microcrystals, from which we have determined the atomic structure of the cross-beta spine. It is a double beta-sheet, with each sheet formed from parallel segments stacked in register. Side chains protruding from the two sheets form a dry, tightly self-complementing steric zipper, bonding the sheets. Within each sheet, every segment is bound to its two neighbouring segments through stacks of both backbone and side-chain hydrogen bonds. The structure illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.

Structure of the cross-beta spine of amyloid-like fibrils.,Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D Nature. 2005 Jun 9;435(7043):773-8. PMID:15944695^[4]

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

References

↑ Stansfield I, Jones KM, Kushnirov VV, Dagkesamanskaya AR, Poznyakovski AI, Paushkin SV, Nierras CR, Cox BS, Ter-Avanesyan MD, Tuite MF. The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 1995 Sep 1;14(17):4365-73. PMID:7556078
↑ Hosoda N, Kobayashi T, Uchida N, Funakoshi Y, Kikuchi Y, Hoshino S, Katada T. Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation. J Biol Chem. 2003 Oct 3;278(40):38287-91. Epub 2003 Aug 15. PMID:12923185 doi:http://dx.doi.org/10.1074/jbc.C300300200
↑ Kobayashi T, Funakoshi Y, Hoshino S, Katada T. The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay. J Biol Chem. 2004 Oct 29;279(44):45693-700. Epub 2004 Aug 26. PMID:15337765 doi:http://dx.doi.org/10.1074/jbc.M405163200
↑ Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D. Structure of the cross-beta spine of amyloid-like fibrils. Nature. 2005 Jun 9;435(7043):773-8. PMID:15944695 doi:nature03680

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yjo"

@@ Line 3: / Line 3: @@
 <StructureSection load='1yjo' size='340' side='right'caption='[[1yjo]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yjo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YJO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1yjo]] is a 1 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=1YJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YJO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yjp|1yjp]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1yjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjo OCA], [https://pdbe.org/1yjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yjo RCSB], [https://www.ebi.ac.uk/pdbsum/1yjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yjo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ERF3_YEAST ERF3_YEAST]] Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.<ref>PMID:7556078</ref> <ref>PMID:12923185</ref> <ref>PMID:15337765</ref>
+[https://www.uniprot.org/uniprot/ERF3_YEAST ERF3_YEAST] Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.<ref>PMID:7556078</ref> <ref>PMID:12923185</ref> <ref>PMID:15337765</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Balbirnie, M]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Eisenberg, D]]
+[[Category: Balbirnie M]]
-[[Category: Grothe, R]]
+[[Category: Eisenberg D]]
-[[Category: Madsen, A O]]
+[[Category: Grothe R]]
-[[Category: Nelson, R]]
+[[Category: Madsen AO]]
-[[Category: Riekel, C]]
+[[Category: Nelson R]]
-[[Category: Sawaya, M R]]
+[[Category: Riekel C]]
-[[Category: Asparagine zipper]]
+[[Category: Sawaya MR]]
-[[Category: Glutamine zipper]]
-[[Category: Keywords beta sheet]]
-[[Category: Protein binding]]
-[[Category: Steric zipper]]

1yjo

From Proteopedia

Revision as of 07:14, 9 August 2023

Structure of NNQQNY from yeast prion Sup35 with zinc acetate

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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