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2rnm

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Revision as of 10:33, 25 December 2014

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

Structural highlights

2rnm is a 5 chain structure with sequence from Podospora anserina. The May 2008 RCSB PDB Molecule of the Month feature on Prions by David S. Goodsell is 10.2210/rcsb_pdb/mom_2008_5. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[Q03689_PODAN] 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 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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Turcq B, Deleu C, Denayrolles M, Begueret J. Two allelic genes responsible for vegetative incompatibility in the fungus Podospora anserina are not essential for cell viability. Mol Gen Genet. 1991 Aug;228(1-2):265-9. PMID:1886611
↑ Deleu C, Clave C, Begueret J. A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina. Genetics. 1993 Sep;135(1):45-52. PMID:8224826
↑ Coustou V, Deleu C, Saupe S, Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9773-8. PMID:9275200
↑ Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science. 2008 Mar 14;319(5869):1523-6. PMID:18339938 doi:319/5869/1523

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/2rnm"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rnm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rnm RCSB], [http://www.ebi.ac.uk/pdbsum/2rnm PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/Q03689_PODAN Q03689_PODAN]] 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 ==

2rnm

From Proteopedia

Revision as of 10:33, 25 December 2014

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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