6ZM0

Crystal structure of MreC from Pseudomonas aeruginosa

This is a non-PDB format compatible entry.

Summary for 6ZM0

• Entry DOI: 10.2210/pdb6zm0/pdb
• Descriptor: Cell shape-determining protein MreC, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: rod-shape bacteria, peptidoglycan, elongasome, cytoskeletal, structural protein
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 1
• Total formula weight: 17893.77

Authors

Contreras-Martel, C.,Dessen, A.,Trindade, D.M. (deposition date: 2020-07-01, release date: 2021-03-17, Last modification date: 2024-06-19)

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

X-RAY DIFFRACTION (1.471 Å)