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- EMDB-41696: Characterization of the Chlamydomonas Flagellar Mastigoneme Filam... -

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Basic information

Entry
Database: EMDB / ID: EMD-41696
TitleCharacterization of the Chlamydomonas Flagellar Mastigoneme Filament Structure at 3.4A
Map data
Sample
  • Organelle or cellular component: Mastigoneme filament
    • Other: MST1
KeywordsMastigoneme / MST1 / flagella / Chlamydomonas / STRUCTURAL PROTEIN
Biological speciesChlamydomonas reinhardtii (plant)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsYue W / Kai Z
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM142959 United States
CitationJournal: J Cell Biol / Year: 2023
Title: Cryo-EM reveals how the mastigoneme assembles and responds to environmental signal changes.
Authors: Yue Wang / Jun Yang / Fangheng Hu / Yuchen Yang / Kaiyao Huang / Kai Zhang /
Abstract: Mastigonemes are thread-like structures adorning the flagella of protists. In Chlamydomonas reinhardtii, filamentous mastigonemes find their roots in the flagella's distal region, associated with the ...Mastigonemes are thread-like structures adorning the flagella of protists. In Chlamydomonas reinhardtii, filamentous mastigonemes find their roots in the flagella's distal region, associated with the channel protein PKD2, implying their potential contribution to external signal sensing and flagellar motility control. Here, we present the single-particle cryo-electron microscopy structure of the mastigoneme at 3.4 Å. The filament unit, MST1, consists of nine immunoglobulin-like domains and six Sushi domains, trailed by an elastic polyproline-II helix. Our structure demonstrates that MST1 subunits are periodically assembled to form a centrosymmetric, non-polar filament. Intriguingly, numerous clustered disulfide bonds within a ladder-like spiral configuration underscore structural resilience. While defects in the mastigoneme structure did not noticeably affect general attributes of cell swimming, they did impact specific swimming properties, particularly under varied environmental conditions such as redox shifts and heightened viscosity. Our findings illuminate the potential role of mastigonemes in flagellar motility and suggest their involvement in diverse environmental responses.
History
DepositionAug 23, 2023-
Header (metadata) releaseOct 25, 2023-
Map releaseOct 25, 2023-
UpdateNov 8, 2023-
Current statusNov 8, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_41696.png

Downloads & links

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Map

FileDownload / File: emd_41696.map.gz / Format: CCP4 / Size: 10.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.33 Å
Density
Contour LevelBy AUTHOR: 1.08
Minimum - Maximum0.0 - 4.360147
Average (Standard dev.)0.040315382 (±0.1960584)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions9092331
Spacing9290331
CellA: 122.35999 Å / B: 119.7 Å / C: 440.22998 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Mastigoneme filament

EntireName: Mastigoneme filament
Components
  • Organelle or cellular component: Mastigoneme filament
    • Other: MST1

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Supramolecule #1: Mastigoneme filament

SupramoleculeName: Mastigoneme filament / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Chlamydomonas reinhardtii (plant)

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Macromolecule #1: MST1

MacromoleculeName: MST1 / type: other / ID: 1 / Classification: other
SequenceString: MAMPRHGRRP ARCSSNRASQ WLLLVLGVAL AASPRFLLLV EAATYTLTLD KLGPTVNPTT SDAVTFTATV ASPDSTTAVF FTLDYGDGVT AETTRTTTGA LSTTPTANLV SAGTYTVTYA SIGTKFVTLR LYDSAVAPGV LLASKTVPIY VEDSTLTATL LQSGVPRLNL ...String:
MAMPRHGRRP ARCSSNRASQ WLLLVLGVAL AASPRFLLLV EAATYTLTLD KLGPTVNPTT SDAVTFTATV ASPDSTTAVF FTLDYGDGVT AETTRTTTGA LSTTPTANLV SAGTYTVTYA SIGTKFVTLR LYDSAVAPGV LLASKTVPIY VEDSTLTATL LQSGVPRLNL AFSGFKGRVS SSTANRADMW ATIQLDTAPG VFESSRIFIG IAPTASTNYD FVIPDQVYNL EGAKTTVLRI YDAPVGGTLL RTFTPAAANA VYVVDPSKYV LTLTVGPTSV TTADQVTFTQ TTTEVSYSAS ATSPILQWRF NWDDPSVVET PLAYPDALTA ASNFPTTATA VSSAAASTFR YTSTGSKNAR LRLYDGANNV IAEKIVVITV SNAGYTLALA KTTADPVTTD DTIAFSAGAK HLSSTSQVWW TIDYGAGESS PRTALTMTNV GAAAPNAIAS LSNQYTSGGT KLATLRIYDR DGVGANTGLL LASTTVTFTV TPVLYALESA VEPFSPIATV AAKWSFRIQR SKATPAGVTE SIKCAFFGAD TGTAPADLAA WLTAANGAGG LTATILPSSI PSDIISFTRT YAAAAASLQG KLQCFIGSTP LWDPYYPTPV FQVLAAAPTY TLSASVTPAV VPVDTATLWT YNIIRSVPVP AGGPSLPILC SFWDGKTGAA PTTDAGWAAL AGSANGKGTS MAPGSTTATC SFTPSYSTTG TATPTLQLIQ NSFALDAATT VGFLSPVYTA PAFATVTAAS YTISSYLNPV TPVAGGAAAV WRIVITRNAA VTASAKTLTC QMPDNGQGGS PADVTADIAV GGTTTVCVFS IAGYTTATPG PYFATVNVVD GAVTTSHITK NFTVLASGTT APTYAVTSVV SPATPVKVST PVTYTFTITR TTAVPAGGIP QPIICEFFNG EGTAPASAAA YWRVSTTIPD ADTVVAVMAP GETTTTCTFT TYYTTVSAGG FTAKLMVFGE SATAAPLLTS LSVTPSQLLA AVHSFATPMV VAAAVVAVES TTISPNYNPT TPYTNIPTYF TFTLLRDPPV PPSASSGVQF ACALYTGQNV NPASAPSAIT DAVYKTFTDV TTAVATDANY FADQQLRVVT MAPGTGRVSC TFPTLYAAAG PFSPKFFVFE YASSTVGANA LAVADTVTSL TSFTTQAAPT FITGPTNVPQ RVPLPKGFRT TCFDGYELIF SNDNYTNGVR VAVDAYPYPV GQCRKCPGGT ATMDGYRCIP CPSGYWSNEG ARECTACPAG TIAKPAALTA RAKYSIDPTT YHFVTHLAMG PESCKKCPKG YFQPNIAGTV CLPCPSGFVS TSGATGCTAC SEGTYHTDGV GTTTPGEATS LDTTDTFGSI YPIIPNTCRQ CPANTYLPLR GQAAIASMNL AAVSSATPCR PCEDGTWSKA GAAGCQKCPP GTYRNTWFSG QLGSPFITAD GVPVATTLTE LGSGCSQCPP GTYAPTFGMS VCLPCPAGTF ASAPGATACQ QCKPGTNSLM GDRTQQMALV VTNAANDFPA LRAYTISGMV AGPAYAKPIV TGPDTNFFMA GKSETCSTNL PGYYTDVDGL PIQLPCKPGT FMPFDTATAN LLDTGLTVDG TQCYTCQTGT FNDEFSQPVC KACWSGSFAS KRGLPTCEIA QPGTFTNVAA AANATFNTAT LIPTGLVKGA QAPTPCGMGY FQSSAETTTC TACAVGTYAD QAGLAACKPC QPGRYQNSIG QRVCKPCDMG TYSRYGGELC TKCPAGTVAS KTGSSQCTPC AAGFYANAPD SATSCRACPR GYYGPYSGAY ADNLGDEFEG PRGCYKCPYD FFADRPGVRQ CTACPPLDLG GGNLVEQCTE DLGSQRCKPC SLLSKPKTAR TEQSPPPPSP SPPPPPPPSP RPPSPNPPSP RPPSPAPPSP NPPPTSPPPS PPPSPPPPRP PPPPPPPPSP PPPNRSPPPP PPASSAINPG GGVNQNGDPV GHRRAILSLM EDEDAEAAQE EQAIVDVDAE MQPQDDE

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 39.2 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 98875
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE

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