6ZLV

MreC

Summary for 6ZLV

• Entry DOI: 10.2210/pdb6zlv/pdb
• EMDB information: 11275
• Descriptor: Rod shape-determining protein MreC (1 entity in total)
• Functional Keywords: bacterial cell wall elongation, structural protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 4
• Total formula weight: 76219.38

Authors

Estrozi, L.F.,Contreras-Martel, C. (deposition date: 2020-07-01, release date: 2021-03-17, Last modification date: 2024-07-10)

Primary citation

Martins, A.,Contreras-Martel, C.,Janet-Maitre, M.,Miyachiro, M.M.,Estrozi, L.F.,Trindade, D.M.,Malospirito, C.C.,Rodrigues-Costa, F.,Imbert, L.,Job, V.,Schoehn, G.,Attree, I.,Dessen, A.
Self-association of MreC as a regulatory signal in bacterial cell wall elongation.
Nat Commun, 12:2987-2987, 2021

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 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.

PubMed: 34016967
DOI: 10.1038/s41467-021-22957-9

Experimental method

ELECTRON MICROSCOPY (3.5 Å)