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- EMDB-25371: Allosteric Regulation of Human Plastins -

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Basic information

Entry
Database: EMDB / ID: EMD-25371
TitleAllosteric Regulation of Human Plastins
Map dataF-actin/Plastin 3-ABD1
Sample
  • Complex: Complex of Plastin3-ABD1 with F-actin
    • Protein or peptide: Actin, alpha skeletal muscle
    • Protein or peptide: Plastin 3
Biological speciesGallus gallus (chicken) / Homo sapiens (human)
Methodhelical reconstruction / cryo EM / Resolution: 5.1 Å
AuthorsZheng W / Schwebach CL / Kudryashova E / Egelman EH / Kudryashov DS
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM122510 United States
CitationJournal: Nat Struct Mol Biol / Year: 2022
Title: Allosteric regulation controls actin-bundling properties of human plastins.
Authors: Christopher L Schwebach / Elena Kudryashova / Richa Agrawal / Weili Zheng / Edward H Egelman / Dmitri S Kudryashov /
Abstract: Plastins/fimbrins are conserved actin-bundling proteins contributing to motility, cytokinesis and other cellular processes by organizing strikingly different actin assemblies as in aligned bundles ...Plastins/fimbrins are conserved actin-bundling proteins contributing to motility, cytokinesis and other cellular processes by organizing strikingly different actin assemblies as in aligned bundles and branched networks. We propose that this ability of human plastins stems from an allosteric communication between their actin-binding domains (ABD1/2) engaged in a tight spatial association. Here we show that ABD2 can bind actin three orders of magnitude stronger than ABD1, unless the domains are involved in an equally strong inhibitory engagement. A mutation mimicking physiologically relevant phosphorylation at the ABD1-ABD2 interface greatly weakened their association, dramatically potentiating actin cross-linking. Cryo-EM reconstruction revealed the ABD1-actin interface and enabled modeling of the plastin bridge and domain separation in parallel bundles. We predict that a strong and tunable allosteric inhibition between the domains allows plastins to modulate the cross-linking strength, contributing to remodeling of actin assemblies of different morphologies defining the unique place of plastins in actin organization.
History
DepositionNov 2, 2021-
Header (metadata) releaseMay 11, 2022-
Map releaseMay 11, 2022-
UpdateJul 6, 2022-
Current statusJul 6, 2022Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_25371.png

Downloads & links

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Map

FileDownload / File: emd_25371.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationF-actin/Plastin 3-ABD1
Voxel sizeX=Y=Z: 1.4 Å
Density
Contour LevelBy AUTHOR: 0.0145
Minimum - Maximum-0.02157235 - 0.129046
Average (Standard dev.)0.0010007044 (±0.0070076343)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 358.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Complex of Plastin3-ABD1 with F-actin

EntireName: Complex of Plastin3-ABD1 with F-actin
Components
  • Complex: Complex of Plastin3-ABD1 with F-actin
    • Protein or peptide: Actin, alpha skeletal muscle
    • Protein or peptide: Plastin 3

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Supramolecule #1: Complex of Plastin3-ABD1 with F-actin

SupramoleculeName: Complex of Plastin3-ABD1 with F-actin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

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Macromolecule #1: Actin, alpha skeletal muscle

MacromoleculeName: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Gallus gallus (chicken)
SequenceString: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTL KYPIEHGIIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE K MTQIMFET FNVPAMYVAI QAVLSLYASG RTTGIVLDSG DGVTHNVPIY ...String:
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTL KYPIEHGIIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE K MTQIMFET FNVPAMYVAI QAVLSLYASG RTTGIVLDSG DGVTHNVPIY EGYALPHAIM RL DLAGRDL TDYLMKILTE RGYSFVTTAE REIVRDIKEK LCYVALDFEN EMATAASSSS LEK SYELPD GQVITIGNER FRCPETLFQP SFIGMESAGI HETTYNSIMK CDIDIRKDLY ANNV MSGGT TMYPGIADRM QKEITALAPS TMKIKIIAPP ERKYSVWIGG SILASLSTFQ QMWIT KQEY DEAGPSIVHR KCF

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Macromolecule #2: Plastin 3

MacromoleculeName: Plastin 3 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG YKVREIIQKL MLDGDRNKDG KISFDEFVYI FQEVKSSDIA KTFRKAINRK EGICALGGTS ELSSEGTQHS YSEEEKYAFV NWINKALEND PDCRHVIPMN PNTDDLFKAV GDGIVLCKMI ...String:
MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG YKVREIIQKL MLDGDRNKDG KISFDEFVYI FQEVKSSDIA KTFRKAINRK EGICALGGTS ELSSEGTQHS YSEEEKYAFV NWINKALEND PDCRHVIPMN PNTDDLFKAV GDGIVLCKMI NLSVPDTIDE RAINKKKLTP FIIQENLNLA LNSASAIGCH VVNIGAEDLR AGKPHLVLGL LWQIIKIGLF ADIELSRNEA LAALLRDGET LEELMKLSPE ELLLRWANFH LENSGWQKIN NFSADIKDSK AYFHLLNQIA PKGQKEGEPR IDINMSGFNE TDDLKRAESM LQQADKLGCR QFVTPADVVS GNPKLNLAFV ANLFNKYPAL TKPENQDIDW TLLEGETREE RTFRNWMNSL GVNPHVNHLY ADLQDALVIL QLYERIKVPV DWSKVNKPPY PKLGANMKKL ENCNYAVELG KHPAKFSLVG IGGQDLNDGN QTLTLALVWQ LMRRYTLNVL EDLGDGQKAN DDIIVNWVNR TLSEAGKSTS IQSFKDKTIS SSLAVVDLID AIQPGCINYD LVKSGNLTED DKHNNAKYAV SMARRIGARV YALPEDLVEV KPKMVMTVFA CLMGRGMKRV

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.5
GridModel: PELCO Ultrathin Carbon with Lacey Carbon / Pretreatment - Type: PLASMA CLEANING
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 20.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 28.0 Å
Applied symmetry - Helical parameters - Δ&Phi: -166.5 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 5.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 155939
CTF correctionSoftware - Name: RELION
Final angle assignmentType: NOT APPLICABLE / Software - Name: RELION

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