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2kj3

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Revision as of 10:55, 18 July 2018

High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

Structural highlights

2kj3 is a 3 chain structure with sequence from Podas. The September 2015 RCSB PDB Molecule of the Month feature on Amyloids by David Goodsell is 10.2210/rcsb_pdb/mom_2015_9. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2rnm
Gene:	small s (PODAS)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

We 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.

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
↑ Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Bockmann A, Meier BH. Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy. J Am Chem Soc. 2010 Sep 9. PMID:20828131 doi:10.1021/ja104213j

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/2kj3"

@@ Line 1: / Line 1: @@
 ==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=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rnm|2rnm]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">small s ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kj3 OCA], [http://pdbe.org/2kj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2kj3 PDBsum]</span></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=2kj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kj3 OCA], [http://pdbe.org/2kj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2kj3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kj3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 [[Category: Podas]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Ab, E]]
+[[Category: AB, E]]
 [[Category: Lange, A]]
 [[Category: Loquet, A]]

2kj3

From Proteopedia

Revision as of 10:55, 18 July 2018

High-resolution 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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