7yat

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CryoEM tetra protofilament structure of the hamster prion 108-144 fibril

Structural highlights

7yat is a 24 chain structure with sequence from Mesocricetus auratus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PRIO_MESAU Note=Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.

Function

PRIO_MESAU May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).[1]

Publication Abstract from PubMed

Fibrils of the hamster prion peptide (sHaPrP, sequence 108-144) were prepared in an acidic solution, and their structure was solved by cryogenic electron microscopy with a resolution of 2.23 A based on the gold-standard Fourier shell correlation (FSC) curve. The fibril has a novel architecture that has never been found in other amyloid fibrils. Each fibril is assembled by four protofilaments (PFs) and has an ordered water channel in the center. Each protofilament contains three beta-strands (125-130, 133-135, and 138-141) arranged in an "R"-shaped construct. The structural data indicate that these three beta-strand segments are the most amyloidogenic region of the prion peptide/protein and might be the site of nucleation during fibrillization under conditions without denaturants.

2.2 A Cryo-EM Tetra-Protofilament Structure of the Hamster Prion 108-144 Fibril Reveals an Ordered Water Channel in the Center.,Chen EH, Kao HW, Lee CH, Huang JYC, Wu KP, Chen RP J Am Chem Soc. 2022 Aug 3;144(30):13888-13894. doi: 10.1021/jacs.2c05479. Epub , 2022 Jul 20. PMID:35857020[2]

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

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Citations
1 reviews cite this structure
Recent advances in infectious disease research using cryo-electron tomography.
Asarnow et al. (2023)
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3 other articles
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See Also

References

  1. ↑ Juanes ME, Elvira G, Garcia-Grande A, Calero M, Gasset M. Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative initiation of translation. J Biol Chem. 2009 Jan 30;284(5):2787-94. doi: 10.1074/jbc.M804051200. Epub 2008, Dec 5. PMID:19059915 doi:10.1074/jbc.M804051200
  2. ↑ Chen EH, Kao HW, Lee CH, Huang JYC, Wu KP, Chen RP. 2.2 A Cryo-EM Tetra-Protofilament Structure of the Hamster Prion 108-144 Fibril Reveals an Ordered Water Channel in the Center. J Am Chem Soc. 2022 Jul 20. doi: 10.1021/jacs.2c05479. PMID:35857020 doi:http://dx.doi.org/10.1021/jacs.2c05479

Contents


PDB ID 7yat

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OCA

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