Open AccessThe crystal structure of MreC provides insights into polymer formation
Author(s) -
Xu Qin,
Sun Ning,
Xiao Qingjie,
Huang Chiaying,
Xu Mengxue,
Zhang Weizhe,
Li Lina,
Wang Qisheng,
Olieric Vincent,
Wang Weiwu,
He Jianhua,
Sun Bo
Publication year - 2022
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.13296
Subject(s) - periplasmic space , coiled coil , antiparallel (mathematics) , protein filament , cryo electron microscopy , biophysics , protein structure , microbiology and biotechnology , crystallography , biology , chemistry , escherichia coli , biochemistry , physics , gene , quantum mechanics , magnetic field
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.