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==High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR== | ==High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR== | ||
<StructureSection load='2kj3' size='340' side='right' caption='[[2kj3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2kj3' size='340' side='right'caption='[[2kj3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kj3]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2kj3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Podas Podas]. The September 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Amyloids'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_9 10.2210/rcsb_pdb/mom_2015_9]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KJ3 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rnm|2rnm]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rnm|2rnm]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">small s ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">small s ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5145 PODAS])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kj3 OCA], [https://pdbe.org/2kj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kj3 RCSB], [https://www.ebi.ac.uk/pdbsum/2kj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kj3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/HETS_PODAS HETS_PODAS]] Responsible for heterokaryon incompatibility, a process that ensures that during spontaneous, vegetative cell fusion only compatible cells from the same colony survive (non-self-recognition). Forms a prion for the non-Mendelian trait [het-s]. Interacts with het-S from incompatible cells to trigger a lethal reaction that prevents the formation of viable heterokaryons. It is unknown if the native, soluble protein has a cellular function.<ref>PMID:1886611</ref> <ref>PMID:8224826</ref> <ref>PMID:9275200</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Prion|Prion]] | *[[Prion 3D structures|Prion 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 27: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Amyloids]] | [[Category: Amyloids]] | ||
[[Category: Large Structures]] | |||
[[Category: Podas]] | [[Category: Podas]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
Revision as of 10:26, 14 April 2021
High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMRHigh-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR
Structural highlights
Function[HETS_PODAS] Responsible for heterokaryon incompatibility, a process that ensures that during spontaneous, vegetative cell fusion only compatible cells from the same colony survive (non-self-recognition). Forms a prion for the non-Mendelian trait [het-s]. Interacts with het-S from incompatible cells to trigger a lethal reaction that prevents the formation of viable heterokaryons. It is unknown if the native, soluble protein has a cellular function.[1] [2] [3] Publication Abstract from PubMedWe present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal prion HET-s in its amyloid form. On the basis of 134 unambiguous distance restraints, we recently showed that HET-s(218-289) in its fibrillar state forms a left-handed beta-solenoid, and an atomic-resolution NMR structure of the triangular core was determined from unambiguous restraints only. In this paper, we go considerably further and present a comprehensive protocol using six differently labeled samples, a collection of optimized solid-state NMR experiments, and adapted structure calculation protocols. The high-resolution structure obtained includes the less ordered but biologically important C-terminal part and improves the overall accuracy by including a large number of ambiguous distance restraints. Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy.,Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Bockmann A, Meier BH J Am Chem Soc. 2010 Sep 9. PMID:20828131[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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