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- EMDB-43274: Structure of full-length gelsolin bound to the barbed end of F-actin -

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Basic information

Entry
Database: EMDB / ID: EMD-43274
TitleStructure of full-length gelsolin bound to the barbed end of F-actin
Map data
Sample
  • Complex: Structure of full-length cytoplasmic gelsolin bound to the barbed end of F-actin
    • Complex: skeletal actin
    • Protein or peptide: Actin, alpha skeletal muscle
    • Protein or peptide: Gelsolin
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: CALCIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
Keywordscytoskeleton / actin / cell motility / PROTEIN BINDING
Function / homology
Function and homology information


striated muscle atrophy / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering / renal protein absorption / positive regulation of keratinocyte apoptotic process / positive regulation of protein processing in phagocytic vesicle / positive regulation of actin nucleation / phosphatidylinositol 3-kinase catalytic subunit binding / actin cap ...striated muscle atrophy / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering / renal protein absorption / positive regulation of keratinocyte apoptotic process / positive regulation of protein processing in phagocytic vesicle / positive regulation of actin nucleation / phosphatidylinositol 3-kinase catalytic subunit binding / actin cap / regulation of podosome assembly / myosin II binding / host-mediated suppression of symbiont invasion / actin filament severing / actin filament capping / barbed-end actin filament capping / actin filament depolymerization / cell projection assembly / actin polymerization or depolymerization / cardiac muscle cell contraction / relaxation of cardiac muscle / Sensory processing of sound by outer hair cells of the cochlea / podosome / cytoskeletal motor activator activity / phagocytosis, engulfment / cortical actin cytoskeleton / myosin heavy chain binding / hepatocyte apoptotic process / tropomyosin binding / actin filament bundle / troponin I binding / filamentous actin / mesenchyme migration / actin filament bundle assembly / skeletal muscle myofibril / striated muscle thin filament / skeletal muscle thin filament assembly / actin monomer binding / sarcoplasm / cilium assembly / Caspase-mediated cleavage of cytoskeletal proteins / skeletal muscle fiber development / stress fiber / phagocytic vesicle / titin binding / response to muscle stretch / phosphatidylinositol-4,5-bisphosphate binding / actin filament polymerization / actin filament organization / central nervous system development / filopodium / actin filament / protein destabilization / cellular response to type II interferon / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / calcium-dependent protein binding / actin filament binding / lamellipodium / actin cytoskeleton / actin binding / cell body / secretory granule lumen / blood microparticle / amyloid fibril formation / ficolin-1-rich granule lumen / hydrolase activity / Amyloid fiber formation / protein domain specific binding / focal adhesion / calcium ion binding / Neutrophil degranulation / positive regulation of gene expression / magnesium ion binding / extracellular space / extracellular exosome / extracellular region / ATP binding / identical protein binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Villin/Gelsolin / Gelsolin homology domain / Gelsolin-like domain / Gelsolin repeat / ADF-H/Gelsolin-like domain superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. ...Villin/Gelsolin / Gelsolin homology domain / Gelsolin-like domain / Gelsolin repeat / ADF-H/Gelsolin-like domain 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
Gelsolin / Actin, alpha skeletal muscle
Similarity search - Component
Biological speciesOryctolagus cuniculus (rabbit) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.63 Å
AuthorsBarrie KR / Rebowski G / Dominguez R
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM073791 United States
CitationJournal: bioRxiv / Year: 2024
Title: Mechanism of Actin Filament Severing and Capping by Gelsolin.
Authors: Kyle R Barrie / Grzegorz Rebowski / Roberto Dominguez
Abstract: Gelsolin is the prototypical member of a family of Ca -dependent F-actin severing and capping proteins. A structure of Ca -bound full-length gelsolin at the barbed end shows domains G1G6 and the ...Gelsolin is the prototypical member of a family of Ca -dependent F-actin severing and capping proteins. A structure of Ca -bound full-length gelsolin at the barbed end shows domains G1G6 and the inter-domain linkers wrapping around F-actin. Another structure shows domains G1G3, a fragment produced during apoptosis, on both sides of F-actin. Conformational changes that trigger severing occur on one side of F-actin with G1G6 and on both sides with G1G3. Gelsolin remains bound after severing, blocking subunit exchange.
History
DepositionJan 5, 2024-
Header (metadata) releaseOct 16, 2024-
Map releaseOct 16, 2024-
UpdateJun 4, 2025-
Current statusJun 4, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_43274.png

Downloads & links

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Map

FileDownload / File: emd_43274.map.gz / Format: CCP4 / Size: 274.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 416 pix.
= 449.28 Å		1.08 Å/pix.
x 416 pix.
= 449.28 Å		1.08 Å/pix.
x 416 pix.
= 449.28 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.05
Minimum - Maximum-0.081286155 - 0.4361192
Average (Standard dev.)0.0023675219 (±0.008571131)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions416416416
Spacing416416416
CellA=B=C: 449.28003 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Structure of full-length cytoplasmic gelsolin bound to the barbed...

EntireName: Structure of full-length cytoplasmic gelsolin bound to the barbed end of F-actin
Components
  • Complex: Structure of full-length cytoplasmic gelsolin bound to the barbed end of F-actin
    • Complex: skeletal actin
    • Protein or peptide: Actin, alpha skeletal muscle
    • Protein or peptide: Gelsolin
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: CALCIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

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Supramolecule #1: Structure of full-length cytoplasmic gelsolin bound to the barbed...

SupramoleculeName: Structure of full-length cytoplasmic gelsolin bound to the barbed end of F-actin
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Oryctolagus cuniculus (rabbit)

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Supramolecule #2: skeletal actin

SupramoleculeName: skeletal actin / type: complex / ID: 2 / Parent: 1
Source (natural)Organism: Oryctolagus cuniculus (rabbit)

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Macromolecule #1: Actin, alpha skeletal muscle

MacromoleculeName: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Oryctolagus cuniculus (rabbit)
Molecular weightTheoretical: 41.875633 KDa
SequenceString: DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IE(HIC)GII TNW DDMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSG DG VTHNVPIYEG ...String:
DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IE(HIC)GII TNW DDMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSG DG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSL E KSYELPDGQV ITIGNERFRC PETLFQPSFI GMESAGIHET TYNSIMKCDI DIRKDLYANN VMSGGTTMYP GIADRMQKE ITALAPSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ITKQEYDEAG PSIVHRKCF

UniProtKB: Actin, alpha skeletal muscle

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Macromolecule #2: Gelsolin

MacromoleculeName: Gelsolin / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 82.73768 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHHMVV EHPEFLKAGK EPGLQIWRVE KFDLVPVPTN LYGDFFTGDA YVILKTVQLR NGNLQYDLHY WLGNECSQDE SGAAAIFTV QLDDYLNGRA VQHREVQGFE SATFLGYFKS GLKYKKGGVA SGFKHVVPNE VVVQRLFQVK GRRVVRATEV P VSWESFNN ...String:
MHHHHHHMVV EHPEFLKAGK EPGLQIWRVE KFDLVPVPTN LYGDFFTGDA YVILKTVQLR NGNLQYDLHY WLGNECSQDE SGAAAIFTV QLDDYLNGRA VQHREVQGFE SATFLGYFKS GLKYKKGGVA SGFKHVVPNE VVVQRLFQVK GRRVVRATEV P VSWESFNN GDCFILDLGN NIHQWCGSNS NRYERLKATQ VSKGIRDNER SGRARVHVSE EGTEPEAMLQ VLGPKPALPA GT EDTAKED AANRKLAKLY KVSNGAGTMS VSLVADENPF AQGALKSEDC FILDHGKDGK IFVWKGKQAN TEERKAALKT ASD FITKMD YPKQTQVSVL PEGGETPLFK QFFKNWRDPD QTDGLGLSYL SSHIANVERV PFDAATLHTS TAMAAQHGMD DDGT GQKQI WRIEGSNKVP VDPATYGQFY GGDSYIILYN YRHGGRQGQI IYNWQGAQST QDEVAASAIL TAQLDEELGG TPVQS RVVQ GKEPAHLMSL FGGKPMIIYK GGTSREGGQT APASTRLFQV RANSAGATRA VEVLPKAGAL NSNDAFVLKT PSAAYL WVG TGASEAEKTG AQELLRVLRA QPVQVAEGSE PDGFWEALGG KAAYRTSPRL KDKKMDAHPP RLFACSNKIG RFVIEEV PG ELMQEDLATD DVMLLDTWDQ VFVWVGKDSQ EEEKTEALTS AKRYIETDPA NRDRRTPITV VKQGFEPPSF VGWFLGWD D DYWSVDPLDR AMAELAAWSH PQFEK

UniProtKB: Gelsolin

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Macromolecule #3: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 5 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #4: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 4 / Number of copies: 14 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #5: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 45.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: OTHER
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.63 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 94956
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: OTHER

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