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2omm

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Revision as of 10:28, 15 March 2023

GNNQQNY peptide corresponding to residues 7-13 of yeast prion sup35

Structural highlights

2omm 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.
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

Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-beta spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of beta-sheets, with the facing side chains of the two sheets interdigitated in a dry 'steric zipper'. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer's amyloid-beta and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, alpha-synuclein and beta(2)-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.

Atomic structures of amyloid cross-beta spines reveal varied steric zippers.,Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJ, McFarlane HT, Madsen AO, Riekel C, Eisenberg D Nature. 2007 May 24;447(7143):453-7. Epub 2007 Apr 29. PMID:17468747^[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
↑ Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJ, McFarlane HT, Madsen AO, Riekel C, Eisenberg D. Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature. 2007 May 24;447(7143):453-7. Epub 2007 Apr 29. PMID:17468747 doi:nature05695

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/2omm"

Categories: Large Structures | Saccharomyces cerevisiae S288C | Eisenberg D | Nelson R | Sawaya MR

@@ Line 3: / Line 3: @@
 <StructureSection load='2omm' size='340' side='right'caption='[[2omm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2omm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OMM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2omm]] 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=2OMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OMM FirstGlance]. <br>
-</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]], [[2olx|2olx]], [[1yjo|1yjo]]</div></td></tr>
+</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=2omm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2omm OCA], [https://pdbe.org/2omm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2omm RCSB], [https://www.ebi.ac.uk/pdbsum/2omm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2omm 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=2omm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2omm OCA], [https://pdbe.org/2omm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2omm RCSB], [https://www.ebi.ac.uk/pdbsum/2omm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2omm 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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 25: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Eisenberg, D]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Nelson, R]]
+[[Category: Eisenberg D]]
-[[Category: Sawaya, M R]]
+[[Category: Nelson R]]
-[[Category: Asparagine zipper]]
+[[Category: Sawaya MR]]
-[[Category: Glutamine zipper]]
-[[Category: Polar zipper]]
-[[Category: Protein fibril]]
-[[Category: Steric zipper]]

2omm

From Proteopedia

Revision as of 10:28, 15 March 2023

GNNQQNY peptide corresponding to residues 7-13 of yeast prion sup35

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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