Open AccessCrystal structure of the N‐terminal domain of MinC dimerized via domain swapping
Author(s) -
An Jun Yop,
Kim Tae Gyun,
Park Kyoung Ryoung,
Lee JungGyu,
Youn HyungSeop,
Lee Youngjin,
Kang Jung Youn,
Kang Gil Bu,
Eom Soo Hyun
Publication year - 2013
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s0909049513022760
Subject(s) - ftsz , dimer , domain (mathematical analysis) , cell division , protein subunit , thermotoga maritima , ring (chemistry) , chemistry , crystallography , c terminus , biophysics , escherichia coli , cell , biology , biochemistry , mathematical analysis , mathematics , organic chemistry , gene , amino acid
Proper cell division at the mid‐site of gram‐negative bacteria reflects critical regulation by the min system (MinC, MinD and MinE) of the cytokinetic Z ring, which is a polymer composed of FtsZ subunits. MinC and MinD act together to inhibit aberrantly positioned Z‐ring formation. MinC consists of two domains: an N‐terminal domain (MinC NTD ), which interacts with FtsZ and inhibits FtsZ polymerization, and a C‐terminal domain (MinC CTD ), which interacts with MinD and inhibits the bundling of FtsZ filaments. These two domains reportedly function together, and both are essential for normal cell division. The full‐length dimeric structure of MinC from Thermotoga maritima has been reported, and shows that MinC dimerization occurs via MinC CTD ; MinC NTD is not involved in dimerization. Here the crystal structure of Escherichia coli MinC NTD ( Eco MinC NTD ) is reported. Eco MinC NTD forms a dimer via domain swapping between the first β strands in each subunit. It is therefore suggested that the dimerization of full‐length Eco MinC occurs via both MinC CTD and MinC NTD , and that the dimerized Eco MinC NTD likely plays an important role in inhibiting aberrant Z‐ring localization.