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1yjp

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Structure of GNNQQNY from yeast prion Sup35

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@@ Line 3: / Line 3: @@
 <StructureSection load='1yjp' size='340' side='right'caption='[[1yjp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yjp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YJP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1yjp]] 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=1YJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YJP FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yjo|1yjo]]</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]] 1.8&#8491;</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=1yjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjp OCA], [http://pdbe.org/1yjp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yjp RCSB], [http://www.ebi.ac.uk/pdbsum/1yjp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yjp ProSAT]</span></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=1yjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjp OCA], [https://pdbe.org/1yjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yjp RCSB], [https://www.ebi.ac.uk/pdbsum/1yjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yjp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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 ==
-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<ref>PMID:15944695</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1yjp" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Prion|Prion]]
+*[[Prion 3D structures|Prion 3D structures]]
 == References ==
 <references/>
@@ Line 26: / Line 17: @@
 </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: Beta sheet]]
-[[Category: Glutamine zipper]]
-[[Category: Protein binding]]
-[[Category: Steric zipper]]

1yjp

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Current revision

Structure of GNNQQNY from yeast prion Sup35

Structural highlights

Function

See Also

References

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