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- EMDB-11275: MreC -

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Basic information

Entry
Database: EMDB / ID: EMD-11275
TitleMreC
Map dataMreC
Sample
  • Complex: MreC
    • Protein or peptide: Rod shape-determining protein MreC
Keywordsbacterial cell wall elongation / STRUCTURAL PROTEIN
Function / homologyCell/Rod shape-determining protein MreC, domain 1 / Rod shape-determining protein MreC / Cell/Rod shape-determining protein MreC, domain 2 / rod shape-determining protein MreC / regulation of cell shape / Cell shape-determining protein MreC
Function and homology information
Biological speciesPseudomonas aeruginosa (bacteria)
Methodhelical reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsEstrozi LF / Contreras-Martel C
Funding support Brazil, France, 7 items
OrganizationGrant numberCountry
Sao Paulo Research Foundation (FAPESP)2011/52067-6 Brazil
Sao Paulo Research Foundation (FAPESP)2017/12436-9 Brazil
French National Research AgencyANR-18-CE11-0019 France
Foundation for Medical Research (France)DEQ20170336705 France
Sao Paulo Research Foundation (FAPESP)2015/19906-5 Brazil
French National Research AgencyANR-10-INBS-05-02 France
French National Research AgencyANR-17-EURE-0003 France
CitationJournal: Nat Commun / Year: 2021
Title: Self-association of MreC as a regulatory signal in bacterial cell wall elongation.
Authors: Alexandre Martins / Carlos Contreras-Martel / Manon Janet-Maitre / Mayara M Miyachiro / Leandro F Estrozi / Daniel Maragno Trindade / Caíque C Malospirito / Fernanda Rodrigues-Costa / ...Authors: Alexandre Martins / Carlos Contreras-Martel / Manon Janet-Maitre / Mayara M Miyachiro / Leandro F Estrozi / Daniel Maragno Trindade / Caíque C Malospirito / Fernanda Rodrigues-Costa / Lionel Imbert / Viviana Job / Guy Schoehn / Ina Attrée / Andréa Dessen /
Abstract: The elongasome, or Rod system, is a protein complex that controls cell wall formation in rod-shaped bacteria. MreC is a membrane-associated elongasome component that co-localizes with the ...The elongasome, or Rod system, is a protein complex that controls cell wall formation in rod-shaped bacteria. MreC is a membrane-associated elongasome component that co-localizes with the cytoskeletal element MreB and regulates the activity of cell wall biosynthesis enzymes, in a process that may be dependent on MreC self-association. Here, we use electron cryo-microscopy and X-ray crystallography to determine the structure of a self-associated form of MreC from Pseudomonas aeruginosa in atomic detail. MreC monomers interact in head-to-tail fashion. Longitudinal and lateral interfaces are essential for oligomerization in vitro, and a phylogenetic analysis of proteobacterial MreC sequences indicates the prevalence of the identified interfaces. Our results are consistent with a model where MreC's ability to alternate between self-association and interaction with the cell wall biosynthesis machinery plays a key role in the regulation of elongasome activity.
History
DepositionJul 1, 2020-
Header (metadata) releaseMar 17, 2021-
Map releaseMar 17, 2021-
UpdateJul 10, 2024-
Current statusJul 10, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.045
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.045
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6zlv
  • Surface level: 0.045
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6zlv
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11275.png

Downloads & links

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Map

FileDownload / File: emd_11275.map.gz / Format: CCP4 / Size: 155.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMreC
Voxel sizeX=Y=Z: 1.206 Å
Density
Contour LevelBy AUTHOR: 0.045 / Movie #1: 0.045
Minimum - Maximum-0.054834697 - 0.17393795
Average (Standard dev.)0.0002928533 (±0.010438674)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-172-172-172
Dimensions344344344
Spacing344344344
CellA=B=C: 414.86398 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.2061.2061.206
M x/y/z344344344
origin x/y/z0.0000.0000.000
length x/y/z414.864414.864414.864
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS-172-172-172
NC/NR/NS344344344
D min/max/mean-0.0550.1740.000

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Supplemental data

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Sample components

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Entire : MreC

EntireName: MreC
Components
  • Complex: MreC
    • Protein or peptide: Rod shape-determining protein MreC

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Supramolecule #1: MreC

SupramoleculeName: MreC / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)

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Macromolecule #1: Rod shape-determining protein MreC

MacromoleculeName: Rod shape-determining protein MreC / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 19.054844 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString:
AALTEQNVRL RELLNSAALV DDKVLVSELI GVDPNPFTQR IMIDKGENDG VFVGQPVLDA SGLMGQVVEV MPYTARVLLL TDTTHSIPV QVNRNGLRAI AVGTGNPERL ELRYVADTAD IKEGDLLVSS GLGQRFPAGY PVATVKEVIH DSGQPFAVVR A VPTAKMNR SRYVLLVF

UniProtKB: Cell shape-determining protein MreC

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statehelical array

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Sample preparation

BufferpH: 8
GridModel: Quantifoil / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. / Details: 30 mA
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 2-20 / Number real images: 1200 / Average electron dose: 43.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.5 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 120000
Sample stageCooling holder cryogen: NITROGEN

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 10.35 Å
Applied symmetry - Helical parameters - Δ&Phi: 62.997637589 °
Applied symmetry - Helical parameters - Axial symmetry: D2 (2x2 fold dihedral)
Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 91840
Segment selectionNumber selected: 111624 / Software - Name: RELION (ver. 3.0)
Startup modelType of model: INSILICO MODEL
In silico model: SPRING (Segclassreconstruct) and Relion 2D class averages.
Final angle assignmentType: NOT APPLICABLE / Software - Name: RELION
FSC plot (resolution estimation)

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