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- PDB-37vy: CTE Type I-like structure -

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Basic information

Entry
Database: PDB / ID: 37vy
TitleCTE Type I-like structure
ComponentsIsoform Tau-F of Microtubule-associated protein tau
KeywordsSTRUCTURAL PROTEIN / Microtubule-associated protein
Function / homologyActivation of AMPK downstream of NMDARs / PKR-mediated signaling / Isoform Tau-F of Microtubule-associated protein tau
Function and homology information
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.96 Å
AuthorsWatanabe, R. / Lee, E.B.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Aging (NIH/NIA) United States
CitationJournal: Biochem Biophys Res Commun / Year: 2026
Title: Structural heterogeneity of CTE Type I tau filaments with an interface-shifted polymorph.
Authors: Ryohei Watanabe / Edward B Lee /
Abstract: Tau filament types can differ in inter-protofilament packing while sharing the same protofilament fold. Motivated by our recent findings in vacuolar tauopathy, we analyzed cryo-electron microscopy ...Tau filament types can differ in inter-protofilament packing while sharing the same protofilament fold. Motivated by our recent findings in vacuolar tauopathy, we analyzed cryo-electron microscopy (cryo-EM) data from brain-derived chronic traumatic encephalopathy (CTE) tau filaments deposited in EMPIAR-10313. We resolved the canonical CTE Type I structure and a previously unreported CTE Type I-like structure with a shifted protofilament interface at 2.78 and 2.96 Å, respectively. Mapping particle-state assignments back onto the original micrographs showed that the CTE Type I and CTE Type I-like packing states can occupy locally contiguous regions within the same fibrils. These findings identify an interface-shifted CTE Type I-like structure and support its local coexistence with CTE Type I within individual fibrils.
History
DepositionAug 9, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 14, 2026Provider: repository / Type: Initial release
Revision 1.0Oct 14, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
D: Isoform Tau-F of Microtubule-associated protein tau
F: Isoform Tau-F of Microtubule-associated protein tau
I: Isoform Tau-F of Microtubule-associated protein tau
B: Isoform Tau-F of Microtubule-associated protein tau
A: Isoform Tau-F of Microtubule-associated protein tau
G: Isoform Tau-F of Microtubule-associated protein tau
K: Isoform Tau-F of Microtubule-associated protein tau
L: Isoform Tau-F of Microtubule-associated protein tau
N: Isoform Tau-F of Microtubule-associated protein tau
E: Isoform Tau-F of Microtubule-associated protein tau
J: Isoform Tau-F of Microtubule-associated protein tau
C: Isoform Tau-F of Microtubule-associated protein tau
H: Isoform Tau-F of Microtubule-associated protein tau
M: Isoform Tau-F of Microtubule-associated protein tau


Theoretical massNumber of molelcules
Total (without water)642,87814
Polymers642,87814
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails (eV)
d_1ens_1chain "J"
d_2ens_1chain "B"
d_3ens_1chain "C"
d_4ens_1chain "D"
d_5ens_1chain "E"
d_6ens_1chain "F"
d_7ens_1chain "G"
d_8ens_1chain "H"
d_9ens_1chain "I"
d_10ens_1chain "A"
d_11ens_1chain "K"
d_12ens_1chain "L"
d_13ens_1chain "M"
d_14ens_1chain "N"

NCS domain segments:

Component-ID: 1 / Ens-ID: ens_1 / Beg auth comp-ID: VAL / Beg label comp-ID: VAL / End auth comp-ID: ARG / End label comp-ID: ARG / Auth seq-ID: 306 - 379 / Label seq-ID: 306 - 379

Dom-IDAuth asym-IDLabel asym-ID
d_1JK
d_2BD
d_3CL
d_4DA
d_5EJ
d_6FB
d_7GF
d_8HM
d_9IC
d_10AE
d_11KG
d_12LH
d_13MN
d_14NI

NCS oper:
IDCodeMatrixVector
1given(-0.999474942978, 0.032369809685, -0.00142610692598), (-0.0323708874091, -0.999475652133, 0.000739217403592), (-0.00140143082319, 0.000784993619037, 0.999998709888)398.756795919, 411.494172484, -6.9680588075
2given(-0.999942413705, 0.0107294344141, -0.00022025057522), (-0.0107295467208, -0.999942304025, 0.000515217735288), (-0.000214709872749, 0.000517551254645, 0.99999984302)402.991635854, 407.255110211, -2.40876113011
3given(-0.999936888421, -0.0111281413329, -0.00154390606434), (0.0111252955985, -0.999936419613, 0.00183970896069), (-0.00156428044352, 0.00182241644241, 0.999997115908)407.648471677, 402.565567547, 2.34965789009
4given(-0.999473276487, -0.0324511873377, -0.000300047992845), (0.0324506325633, -0.999471896025, 0.00169867668064), (-0.000355013611497, 0.00168804520052, 0.999998512233)411.629539733, 398.171246962, 6.88628984218
5given(-0.998489132208, -0.0549492314324, -0.000186621813001), (0.0549493299443, -0.998488980543, -0.000571728117109), (-0.000154923803187, -0.000581119055089, 0.99999981915)415.96429308, 393.891900968, 11.958951512
6given(-0.997095529591, -0.0761604197081, -0.000308770403), (0.0761597022692, -0.997093827663, 0.00189699395248), (-0.000452348918601, 0.00186796832772, 0.999998153036)419.98289144, 388.817375995, 16.3249215146
7given(0.999109953618, -0.0421783003458, 0.00053996351333), (0.0421783440224, 0.99911009525, -6.97527916816E-5), (-0.000536540943037, 9.24654752865E-5, 0.999999851787)8.61005614497, -8.40068254883, -9.37547874765
8given(0.99978382475, -0.0207894217681, 0.000322042866075), (0.0207893933465, 0.999783873034, 9.13519052697E-5), (-0.000323872417215, -8.46370814314E-5, 0.999999943972)4.20899458719, -4.21186651003, -4.64875843135
9given(-0.998615873438, 0.0525942452281, 0.000427419174814), (-0.0525932244993, -0.998613758607, 0.00212458423192), (0.000538567572763, 0.00209916418583, 0.999997651725)394.09687176, 415.107324507, -12.3347678199
10given(0.999743543216, 0.02264254797, -0.000403508516468), (-0.0226426744747, 0.999743573175, -0.000311750269432), (0.00039634622563, 0.000320806830947, 0.999999869996)-4.39939206937, 4.69072428348, 4.61280677286
11given(0.999085474807, 0.042757577234, -6.01598908073E-5), (-0.0427575906578, 0.999085446476, -0.000243067204924), (4.97119065795E-5, 0.000245417205827, 0.99999996865)-8.41880063406, 8.88900266076, 9.41305175018
12given(0.997878697304, 0.0650990854075, 0.000463191604723), (-0.0650985814212, 0.997878305399, -0.00103068476138), (-0.000529305488905, 0.000998345250626, 0.999999361571)-12.8369561943, 13.7687654119, 14.1351099693
13given(0.996414426038, 0.0845986092564, 0.00116914307125), (-0.0846005957508, 0.996413372544, 0.00176924090692), (-0.00101527447045, -0.00186180736314, 0.999997751443)-16.6402951971, 17.5076064978, 19.4866890897

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Components

#1: Protein
Isoform Tau-F of Microtubule-associated protein tau / Neurofibrillary tangle protein / Paired helical filament-tau / PHF-tau


Mass: 45919.871 Da / Num. of mol.: 14 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P10636-8
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: Extracted patient's brain tissue homogenates. / Type: TISSUE / Entity ID: all / Source: NATURAL
Source (natural)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2800 nm / Nominal defocus min: 1700 nm
Image recordingElectron dose: 55.48 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1RELION5.0.0particle selection
13RELION5.0.03D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: 179.4 ° / Axial rise/subunit: 2.37 Å / Axial symmetry: C1
3D reconstructionResolution: 2.96 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 42256 / Symmetry type: HELICAL
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 50.73 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00518078
ELECTRON MICROSCOPYf_angle_d0.538310808
ELECTRON MICROSCOPYf_chiral_restr0.04521218
ELECTRON MICROSCOPYf_plane_restr0.00381372
ELECTRON MICROSCOPYf_dihedral_angle_d12.71443108
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2KJELECTRON MICROSCOPYNCS constraints3.60662611074E-13
ens_1d_3KJELECTRON MICROSCOPYNCS constraints1.21634094531E-13
ens_1d_4KJELECTRON MICROSCOPYNCS constraints3.56214836738E-13
ens_1d_5KJELECTRON MICROSCOPYNCS constraints3.77763129748E-13
ens_1d_6KJELECTRON MICROSCOPYNCS constraints5.23057236466E-13
ens_1d_7KJELECTRON MICROSCOPYNCS constraints2.37494187188E-12
ens_1d_8KJELECTRON MICROSCOPYNCS constraints6.75898328069E-13
ens_1d_9KJELECTRON MICROSCOPYNCS constraints2.45372455669E-13
ens_1d_10KJELECTRON MICROSCOPYNCS constraints1.26730927746E-12
ens_1d_11KJELECTRON MICROSCOPYNCS constraints4.296965663E-13
ens_1d_12KJELECTRON MICROSCOPYNCS constraints1.22226032254E-11
ens_1d_13KJELECTRON MICROSCOPYNCS constraints1.43567810672E-11
ens_1d_14KJELECTRON MICROSCOPYNCS constraints3.38158459251E-13

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