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- PDB-37vx: CTE Type I structure -

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Basic information

Entry
Database: PDB / ID: 37vx
TitleCTE Type I 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: 2.78 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
L: Isoform Tau-F of Microtubule-associated protein tau
N: Isoform Tau-F of Microtubule-associated protein tau
G: Isoform Tau-F of Microtubule-associated protein tau
F: Isoform Tau-F of Microtubule-associated protein tau
K: Isoform Tau-F of Microtubule-associated protein tau
E: Isoform Tau-F of Microtubule-associated protein tau
D: Isoform Tau-F of Microtubule-associated protein tau
H: 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
C: Isoform Tau-F of Microtubule-associated protein tau
A: Isoform Tau-F of Microtubule-associated protein tau
J: 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 "A"
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 "J"
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_1AL
d_2BJ
d_3CK
d_4DG
d_5EF
d_6FD
d_7GC
d_8HH
d_9II
d_10JM
d_11KE
d_12LA
d_13MN
d_14NB

NCS oper:
IDCodeMatrixVector
1given(0.999775865725, 0.021168505315, 0.000335703008594), (-0.0211688516594, 0.999775348489, 0.00106408309443), (-0.000313102543766, -0.00107095104412, 0.999999377515)-4.33412276224, 4.10282669505, 5.0484587546
2given(0.99916633667, 0.0408086093876, -0.00113537024473), (-0.0408102322852, 0.999165870632, -0.00144495863946), (0.00107545644637, 0.00149008875384, 0.999998311513)-7.86353324069, 8.70092023228, 8.91828169124
3given(0.998079791536, 0.0619378411464, -0.000658454551053), (-0.061939138531, 0.998077553886, -0.00217705010584), (0.000522346924036, 0.00221365382346, 0.999997413442)-12.0242592467, 13.3662804879, 13.6211038411
4given(0.996576520471, 0.0826714956918, 0.000814030406473), (-0.0826720558165, 0.99657657429, 0.000680266822056), (-0.000755004958202, -0.000745235509717, 0.999999437296)-16.227169274, 17.2979529577, 19.2615805446
5given(0.994727970582, 0.102548699494, -0.000169629779215), (-0.102548580048, 0.994727813196, 0.000605296452892), (0.000230807823384, -0.000584710019193, 0.999999802421)-19.6856225417, 21.6990090471, 23.7759250722
6given(0.99246782913, 0.12250233954, 0.000885973700644), (-0.122502375601, 0.992468220038, -1.36546130359E-5), (-0.000880973463721, -9.49821188919E-5, 0.999999607432)-23.4410908682, 26.3154614953, 28.623543818
7given(-0.999938511594, -0.0110833978237, -0.000362384994065), (0.0110833255767, -0.999938557905, 0.000200769328796), (-0.000364587934713, 0.000196740552937, 0.999999914184)407.461714865, 402.855210216, 2.40623580286
8given(-0.999547840649, -0.0300670960561, -0.000289807245151), (0.0300675036679, -0.999546709843, -0.00152317621954), (-0.000243878392675, -0.00153120128158, 0.999998797972)411.189065692, 399.302314973, 7.51167379358
9given(-0.998682418941, -0.0513130672403, 0.000628672017603), (0.051313844371, -0.998681744274, 0.00128958508923), (0.00056167070072, 0.00132014553442, 0.99999897087)415.120256556, 394.249630509, 11.436703688
10given(-0.997379386825, -0.0723488669954, 1.34892692224E-5), (0.0723488538336, -0.997379052995, 0.000817310068539), (-4.56775428801E-5, 0.000816144148172, 0.999999665911)419.243822972, 389.800008492, 16.4152876005
11given(-0.995701050491, -0.0926217320751, -0.000795485729268), (0.0926221882862, -0.995701169955, -0.000557124961078), (-0.000740464192437, -0.000628409537995, 0.999999528407)423.196562747, 385.639214149, 21.603869416
12given(-0.993674945798, -0.112294560862, 0.00018356215058), (0.112294468414, -0.99367486957, -0.000453814930616), (0.000233362044382, -0.000430331512462, 0.999999880178)426.549617027, 381.226612637, 26.1089594236
13given(-0.991088845328, -0.133202171011, -0.000286887557158), (0.133201781383, -0.991088324242, 0.00110407806906), (-0.000431396504033, 0.00105602552495, 0.999999349353)430.345909148, 376.169623789, 30.6517739904

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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 symmerty
IDImage processing-IDAngular rotation/subunit (°)Axial rise/subunit (Å)Axial symmetry
11179.42.37C1
21179.42.37C1
3D reconstructionResolution: 2.78 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 33415 / Symmetry type: HELICAL
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 99.65 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00168078
ELECTRON MICROSCOPYf_angle_d0.439910808
ELECTRON MICROSCOPYf_chiral_restr0.04671218
ELECTRON MICROSCOPYf_plane_restr0.00261372
ELECTRON MICROSCOPYf_dihedral_angle_d10.52013108
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2LAELECTRON MICROSCOPYNCS constraints8.87456913679E-11
ens_1d_3LAELECTRON MICROSCOPYNCS constraints9.35577300847E-12
ens_1d_4LAELECTRON MICROSCOPYNCS constraints2.31643163528E-12
ens_1d_5LAELECTRON MICROSCOPYNCS constraints1.07811919095E-13
ens_1d_6LAELECTRON MICROSCOPYNCS constraints3.43096972678E-12
ens_1d_7LAELECTRON MICROSCOPYNCS constraints2.04865104854E-13
ens_1d_8LAELECTRON MICROSCOPYNCS constraints2.09661919888E-12
ens_1d_9LAELECTRON MICROSCOPYNCS constraints4.35627562296E-12
ens_1d_10LAELECTRON MICROSCOPYNCS constraints4.29235292416E-12
ens_1d_11LAELECTRON MICROSCOPYNCS constraints1.25948020841E-13
ens_1d_12LAELECTRON MICROSCOPYNCS constraints1.65409692342E-12
ens_1d_13LAELECTRON MICROSCOPYNCS constraints1.06723957328E-12
ens_1d_14LAELECTRON MICROSCOPYNCS constraints3.2744029374E-12

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