2rnm

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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==
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<StructureSection load='2rnm' size='340' side='right'caption='[[2rnm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2rnm' size='340' side='right'caption='[[2rnm]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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 ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2rnm" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Podas]]
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[[Category: Podospora anserina]]
[[Category: Prions]]
[[Category: Prions]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Lange, A]]
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[[Category: Lange A]]
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[[Category: Meier, B H]]
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[[Category: Meier BH]]
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[[Category: Melckebeke, H Van]]
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[[Category: Riek R]]
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[[Category: Riek, R]]
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[[Category: Siemer A]]
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[[Category: Siemer, A]]
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[[Category: Van Melckebeke H]]
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[[Category: Wasmer, C]]
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[[Category: Wasmer C]]
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[[Category: Amyloid fibril]]
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[[Category: Asparagine ladder]]
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[[Category: Beta-helix]]
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[[Category: Beta-solenoid]]
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[[Category: Hydrophobic core]]
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[[Category: Parallel beta-sheet]]
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[[Category: Prion]]
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[[Category: Protein fibril]]
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[[Category: Salt bridge]]
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Current revision

Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

PDB ID 2rnm

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