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==Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR==
==Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR==
<StructureSection load='2rnm' size='340' side='right'caption='[[2rnm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2rnm' size='340' side='right'caption='[[2rnm]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2rnm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Podas Podas]. The May 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Prions''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_5 10.2210/rcsb_pdb/mom_2008_5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RNM FirstGlance]. <br>
<table><tr><td colspan='2'>[[2rnm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. The May 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Prions''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_5 10.2210/rcsb_pdb/mom_2008_5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RNM FirstGlance]. <br>
</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=2rnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rnm OCA], [https://pdbe.org/2rnm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rnm RCSB], [https://www.ebi.ac.uk/pdbsum/2rnm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rnm ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2rnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rnm OCA], [https://pdbe.org/2rnm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rnm RCSB], [https://www.ebi.ac.uk/pdbsum/2rnm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rnm 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> 
[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;">
== Publication Abstract from PubMed ==
Prion and nonprion forms of proteins are believed to differ solely in their three-dimensional structure, which is therefore of paramount importance for the prion function. However, no atomic-resolution structure of the fibrillar state that is likely infectious has been reported to date. We present a structural model based on solid-state nuclear magnetic resonance restraints for amyloid fibrils from the prion-forming domain (residues 218 to 289) of the HET-s protein from the filamentous fungus Podospora anserina. On the basis of 134 intra- and intermolecular experimental distance restraints, we find that HET-s(218-289) forms a left-handed beta solenoid, with each molecule forming two helical windings, a compact hydrophobic core, at least 23 hydrogen bonds, three salt bridges, and two asparagine ladders. The structure is likely to have broad implications for understanding the infectious amyloid state.
 
Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core.,Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH Science. 2008 Mar 14;319(5869):1523-6. PMID:18339938<ref>PMID:18339938</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rnm" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Podas]]
[[Category: Podospora anserina]]
[[Category: Prions]]
[[Category: Prions]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Lange, A]]
[[Category: Lange A]]
[[Category: Meier, B H]]
[[Category: Meier BH]]
[[Category: Melckebeke, H Van]]
[[Category: Riek R]]
[[Category: Riek, R]]
[[Category: Siemer A]]
[[Category: Siemer, A]]
[[Category: Van Melckebeke H]]
[[Category: Wasmer, C]]
[[Category: Wasmer C]]
[[Category: Amyloid fibril]]
[[Category: Asparagine ladder]]
[[Category: Beta-helix]]
[[Category: Beta-solenoid]]
[[Category: Hydrophobic core]]
[[Category: Parallel beta-sheet]]
[[Category: Prion]]
[[Category: Protein fibril]]
[[Category: Salt bridge]]
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