7EFT

Crystal structure of cell shape-determining protein MreC

Summary for 7EFT

• Entry DOI: 10.2210/pdb7eft/pdb
• Descriptor: Cell shape protein MreC, CHLORIDE ION (3 entities in total)
• Functional Keywords: scaffold protein, dimer, filament-like structure, structural protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 79207.38

Authors

Xu, Q.,Xiao, Q.J.,Sun, B. (deposition date: 2021-03-23, release date: 2021-10-20, Last modification date: 2024-10-23)

Primary citation

Xu, Q.,Sun, N.,Xiao, Q.,Huang, C.Y.,Xu, M.,Zhang, W.,Li, L.,Wang, Q.,Olieric, V.,Wang, W.,He, J.,Sun, B.
The crystal structure of MreC provides insights into polymer formation.
Febs Open Bio, 12:340-348, 2022

PubMed Abstract: MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled-coil domain and two six-stranded barrel domains. The coiled-coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β-barrel domains. In addition, MreC forms an antiparallel filament-like structure along the coiled-coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC.

PubMed: 34510818
DOI: 10.1002/2211-5463.13296

Experimental method

X-RAY DIFFRACTION (2.1 Å)