+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-11275 | ||||||||||||||||||||||||
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Title | MreC | ||||||||||||||||||||||||
Map data | MreC | ||||||||||||||||||||||||
Sample |
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Keywords | bacterial cell wall elongation / STRUCTURAL PROTEIN | ||||||||||||||||||||||||
Function / homology | Cell/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 species | Pseudomonas aeruginosa (bacteria) | ||||||||||||||||||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.5 Å | ||||||||||||||||||||||||
Authors | Estrozi LF / Contreras-Martel C | ||||||||||||||||||||||||
Funding support | Brazil, France, 7 items
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Citation | Journal: 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 |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_11275.map.gz | 141.4 MB | EMDB map data format | |
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Header (meta data) | emd-11275-v30.xml emd-11275.xml | 13.2 KB 13.2 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_11275_fsc.xml | 12.2 KB | Display | FSC data file |
Images | emd_11275.png | 85.7 KB | ||
Filedesc metadata | emd-11275.cif.gz | 5.6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11275 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11275 | HTTPS FTP |
-Validation report
Summary document | emd_11275_validation.pdf.gz | 718.2 KB | Display | EMDB validaton report |
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Full document | emd_11275_full_validation.pdf.gz | 717.7 KB | Display | |
Data in XML | emd_11275_validation.xml.gz | 12.8 KB | Display | |
Data in CIF | emd_11275_validation.cif.gz | 17.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11275 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11275 | HTTPS FTP |
-Related structure data
Related structure data | 6zlvMC 6zm0C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_11275.map.gz / Format: CCP4 / Size: 155.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | MreC | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.206 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : MreC
Entire | Name: MreC |
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Components |
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-Supramolecule #1: MreC
Supramolecule | Name: MreC / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Pseudomonas aeruginosa (bacteria) |
-Macromolecule #1: Rod shape-determining protein MreC
Macromolecule | Name: Rod shape-determining protein MreC / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: Pseudomonas aeruginosa (bacteria) |
Molecular weight | Theoretical: 19.054844 KDa |
Recombinant expression | Organism: Escherichia coli BL21(DE3) (bacteria) |
Sequence | String: 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 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | helical array |
-Sample preparation
Buffer | pH: 8 |
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Grid | Model: Quantifoil / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. / Details: 30 mA |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film 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 beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination 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 stage | Cooling holder cryogen: NITROGEN |