2omm: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2omm.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2omm", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2omm|  PDB=2omm  |  SCENE=  }}
'''GNNQQNY peptide corresponding to residues 7-13 of yeast prion sup35'''


==GNNQQNY peptide corresponding to residues 7-13 of yeast prion sup35==
<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 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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 ==
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.


==Overview==
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<ref>PMID:17468747</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OMM OCA].
</div>
<div class="pdbe-citations 2omm" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17468747 17468747]
*[[Prion 3D structures|Prion 3D structures]]
[[Category: Eisenberg, D.]]
== References ==
[[Category: Nelson, R.]]
<references/>
[[Category: Sawaya, M R.]]
__TOC__
[[Category: Asparagine zipper]]
</StructureSection>
[[Category: Glutamine zipper]]
[[Category: Large Structures]]
[[Category: Polar zipper]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Steric zipper]]
[[Category: Eisenberg D]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:13:33 2008''
[[Category: Nelson R]]
[[Category: Sawaya MR]]

Latest revision as of 10:43, 30 August 2023

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

2omm, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2omm&oldid=3853022"