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- PDB-7utj: Cryogenic electron microscopy 3D map of F-actin bound by human di... -

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Basic information

Entry
Database: PDB / ID: 7utj
TitleCryogenic electron microscopy 3D map of F-actin bound by human dimeric alpha-catenin
Components
  • Actin, alpha skeletal muscle
  • Catenin alpha-1
KeywordsCELL ADHESION / alpha-catenin / F-actin / F-actin binding protein / cell-cell junction
Function / homology
Function and homology information


negative regulation of integrin-mediated signaling pathway / CDH11 homotypic and heterotypic interactions / Regulation of CDH19 Expression and Function / Regulation of CDH11 function / gap junction assembly / epithelial cell-cell adhesion / zonula adherens / gamma-catenin binding / cellular response to indole-3-methanol / vinculin binding ...negative regulation of integrin-mediated signaling pathway / CDH11 homotypic and heterotypic interactions / Regulation of CDH19 Expression and Function / Regulation of CDH11 function / gap junction assembly / epithelial cell-cell adhesion / zonula adherens / gamma-catenin binding / cellular response to indole-3-methanol / vinculin binding / flotillin complex / negative regulation of cell motility / apical junction assembly / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / positive regulation of smoothened signaling pathway / Adherens junctions interactions / catenin complex / negative regulation of protein localization to nucleus / axon regeneration / negative regulation of neuroblast proliferation / cytoskeletal motor activator activity / smoothened signaling pathway / establishment or maintenance of cell polarity / tropomyosin binding / myosin heavy chain binding / Myogenesis / mesenchyme migration / troponin I binding / odontogenesis of dentin-containing tooth / actin filament bundle / filamentous actin / actin filament bundle assembly / skeletal muscle thin filament assembly / striated muscle thin filament / neuroblast proliferation / skeletal muscle myofibril / actin monomer binding / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / intercalated disc / RHO GTPases activate IQGAPs / skeletal muscle fiber development / stress fiber / ovarian follicle development / titin binding / extrinsic apoptotic signaling pathway in absence of ligand / actin filament polymerization / acrosomal vesicle / VEGFR2 mediated vascular permeability / filopodium / integrin-mediated signaling pathway / actin filament / adherens junction / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / protein localization / cell-cell adhesion / beta-catenin binding / response to estrogen / male gonad development / calcium-dependent protein binding / cell migration / actin filament binding / cell-cell junction / actin cytoskeleton / cell junction / lamellipodium / cell body / cell adhesion / hydrolase activity / cadherin binding / protein domain specific binding / focal adhesion / intracellular membrane-bounded organelle / calcium ion binding / positive regulation of gene expression / structural molecule activity / magnesium ion binding / RNA binding / ATP binding / identical protein binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Alpha-catenin / Vinculin, conserved site / Vinculin family talin-binding region signature. / Vinculin/alpha-catenin / Vinculin family / Alpha-catenin/vinculin-like superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site ...Alpha-catenin / Vinculin, conserved site / Vinculin family talin-binding region signature. / Vinculin/alpha-catenin / Vinculin family / Alpha-catenin/vinculin-like superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / Catenin alpha-1 / Actin, alpha skeletal muscle
Similarity search - Component
Biological speciesOryctolagus cuniculus (rabbit)
Homo sapiens (human)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.77 Å
AuthorsRangarajan, E.S. / Smith, E.W. / Izard, T.
Funding support United States, 1items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States) United States
CitationJournal: Commun Biol / Year: 2023
Title: Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments.
Authors: Erumbi S Rangarajan / Emmanuel W Smith / Tina Izard /
Abstract: Attachment between cells is crucial for almost all aspects of the life of cells. These inter-cell adhesions are mediated by the binding of transmembrane cadherin receptors of one cell to cadherins of ...Attachment between cells is crucial for almost all aspects of the life of cells. These inter-cell adhesions are mediated by the binding of transmembrane cadherin receptors of one cell to cadherins of a neighboring cell. Inside the cell, cadherin binds β-catenin, which interacts with α-catenin. The transitioning of cells between migration and adhesion is modulated by α-catenin, which links cell junctions and the plasma membrane to the actin cytoskeleton. At cell junctions, a single β-catenin/α-catenin heterodimer slips along filamentous actin in the direction of cytoskeletal tension which unfolds clustered heterodimers to form catch bonds with F-actin. Outside cell junctions, α-catenin dimerizes and links the plasma membrane to F-actin. Under cytoskeletal tension, α-catenin unfolds and forms an asymmetric catch bond with F-actin. To understand the mechanism of this important α-catenin function, we determined the 2.7 Å cryogenic electron microscopy (cryoEM) structures of filamentous actin alone and bound to human dimeric α-catenin. Our structures provide mechanistic insights into the role of the α-catenin interdomain interactions in directing α-catenin function and suggest a bivalent mechanism. Further, our cryoEM structure of human monomeric α-catenin provides mechanistic insights into α-catenin autoinhibition. Collectively, our structures capture the initial α-catenin interaction with F-actin before the sensing of force, which is a crucial event in cell adhesion and human disease.
History
DepositionApr 27, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 8, 2023Provider: repository / Type: Initial release
Revision 1.1Mar 29, 2023Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Actin, alpha skeletal muscle
B: Actin, alpha skeletal muscle
C: Actin, alpha skeletal muscle
D: Actin, alpha skeletal muscle
E: Actin, alpha skeletal muscle
F: Actin, alpha skeletal muscle
G: Catenin alpha-1
H: Catenin alpha-1
I: Catenin alpha-1
K: Catenin alpha-1
L: Catenin alpha-1
Z: Catenin alpha-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)844,66524
Polymers841,95612
Non-polymers2,70912
Water37821
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_5551
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1chain "B"
d_2ens_1chain "D"
d_3ens_1chain "C"
d_4ens_1chain "A"
d_5ens_1chain "E"
d_6ens_1chain "F"
d_1ens_2chain "I"
d_2ens_2chain "H"
d_3ens_2chain "G"
d_4ens_2chain "K"
d_5ens_2chain "L"
d_6ens_2chain "Z"

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg label comp-IDEnd label comp-IDLabel asym-IDLabel seq-ID
d_11ens_1THRCYSC1 - 370
d_12ens_1ADPADPD
d_21ens_1THRCYSG1 - 370
d_22ens_1ADPADPH
d_31ens_1THRCYSE1 - 370
d_32ens_1ADPADPF
d_41ens_1THRCYSA1 - 370
d_42ens_1ADPADPB
d_51ens_1THRCYSI1 - 370
d_52ens_1ADPADPJ
d_61ens_1THRCYSK1 - 370
d_62ens_1ADPADPL
d_11ens_2ASNLYSO1 - 156
d_21ens_2ASNLYSN1 - 156
d_31ens_2ASNLYSM1 - 156
d_41ens_2ASNLYSV1 - 156
d_51ens_2ASNLYSW1 - 156
d_61ens_2ASNLYSY1 - 156

NCS ensembles :
ID
ens_1
ens_2

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Components

#1: Protein
Actin, alpha skeletal muscle / / Alpha-actin-1


Mass: 42109.973 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: ACTA1, ACTA / Production host: Escherichia coli (E. coli) / References: UniProt: P68135
#2: Protein
Catenin alpha-1 / / Alpha E-catenin / Cadherin-associated protein / Renal carcinoma antigen NY-REN-13


Mass: 98216.031 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CTNNA1 / Production host: Escherichia coli (E. coli) / References: UniProt: P35221
#3: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 21 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: dimeric alpha-catenin (residues 22-906) complexed with F-actin
Type: COMPLEX / Entity ID: #1-#2 / Source: MULTIPLE SOURCES
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
Buffer component
IDConc.NameFormulaBuffer-ID
1150 mMSodium ChlorideNaClSodium chloride1
220 mMTrisTris1
31 mMDithiothreitolDTT1
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: C-flat-1.2/1.3
VitrificationInstrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 65 % / Chamber temperature: 294.15 K

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Electron microscopy imaging

MicroscopyModel: JEOL CRYO ARM 300
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 60000 X / Nominal defocus max: 3000 nm / Nominal defocus min: 500 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: JEOL CRYOSPECPORTER
Image recordingAverage exposure time: 0.1 sec. / Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 2
EM imaging opticsEnergyfilter name: In-column Omega Filter / Phase plate: OTHER

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Processing

Software
NameVersionClassification
phenix.real_space_refine1.18.2_3874refinement
PHENIX1.18.2_3874refinement
EM software
IDNameCategory
2SerialEMimage acquisition
4cryoSPARCCTF correction
7UCSF Chimeramodel fitting
9Cootmodel refinement
10PHENIXmodel refinement
11cryoSPARCinitial Euler assignment
12cryoSPARCfinal Euler assignment
14cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: -166.7 ° / Axial rise/subunit: 27.5 Å / Axial symmetry: C2
3D reconstructionResolution: 2.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 403663 / Symmetry type: HELICAL
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL
Atomic model buildingPDB-ID: 6UPV

6upv


Accession code: 6UPV / Source name: PDB / Type: experimental model
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 40.31 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00925020
ELECTRON MICROSCOPYf_angle_d0.83833840
ELECTRON MICROSCOPYf_dihedral_angle_d19.7793462
ELECTRON MICROSCOPYf_chiral_restr0.0533834
ELECTRON MICROSCOPYf_plane_restr0.0054290
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2DELECTRON MICROSCOPYNCS constraints0.000702381238155
ens_1d_3CELECTRON MICROSCOPYNCS constraints0.000710862280706
ens_1d_4AELECTRON MICROSCOPYNCS constraints0.000711545714394
ens_1d_5EELECTRON MICROSCOPYNCS constraints0.000702825208095
ens_1d_6FELECTRON MICROSCOPYNCS constraints0.000713667347778
ens_2d_2HELECTRON MICROSCOPYNCS constraints0.000702049697677
ens_2d_3GELECTRON MICROSCOPYNCS constraints0.000703963170495
ens_2d_4KELECTRON MICROSCOPYNCS constraints0.000712613282294
ens_2d_5LELECTRON MICROSCOPYNCS constraints0.000715126235944
ens_2d_6ZELECTRON MICROSCOPYNCS constraints0.000711800658507

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