Structural highlights
Publication Abstract from PubMed
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 A 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 beta-barrel domains. In addition, MreC forms an antiparallel filament-like structure along the coiled coil direction, which is different to the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC.
The crystal structure of MreC provides insights into polymer formation.,Xu Q, Sun N, Xiao Q, Huang CY, Xu M, Zhang W, Li L, Wang Q, Olieric V, Wang W, He J, Sun B FEBS Open Bio. 2021 Sep 12. doi: 10.1002/2211-5463.13296. PMID:34510818[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu Q, Sun N, Xiao Q, Huang CY, 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. 2021 Sep 12. doi: 10.1002/2211-5463.13296. PMID:34510818 doi:http://dx.doi.org/10.1002/2211-5463.13296
