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-Structure paper
Title | Self-association of MreC as a regulatory signal in bacterial cell wall elongation. |
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Journal, issue, pages | Nat Commun, Vol. 12, Issue 1, Page 2987, Year 2021 |
Publish date | May 20, 2021 |
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 / |
PubMed 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. |
External links | Nat Commun / PubMed:34016967 / PubMed Central |
Methods | EM (helical sym.) / X-ray diffraction |
Resolution | 1.471 - 3.5 Å |
Structure data | EMDB-11275, PDB-6zlv: PDB-6zm0: |
Chemicals | ChemComp-MG: ChemComp-CL: ChemComp-HOH: |
Source |
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Keywords | STRUCTURAL PROTEIN / bacterial cell wall elongation / Rod-Shape Bacteria / Peptidoglycan / elongasome / cytoskeletal |