title: Crystal structure of the N-terminal domain of MinC dimerized via domain swapping.
abstract: 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 (MinCNTD), which interacts with FtsZ and inhibits FtsZ polymerization, and a C-terminal domain (MinCCTD), 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 MinCCTD; MinCNTD is not involved in dimerization. Here the crystal structure of Escherichia coli MinCNTD (EcoMinCNTD) is reported. EcoMinCNTD forms a dimer via domain swapping between the first β strands in each subunit. It is therefore suggested that the dimerization of full-length EcoMinC occurs via both MinCCTD and MinCNTD, and that the dimerized EcoMinCNTD likely plays an important role in inhibiting aberrant Z-ring localization.
authors.affiliation: School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea.
authors.forename: Jun Yop
authors.initials: JY
authors.lastname: An
authors.forename: Tae Gyun
authors.initials: TG
authors.lastname: Kim
authors.forename: Kyoung Ryoung
authors.initials: KR
authors.lastname: Park
authors.forename: Jung Gyu
authors.initials: JG
authors.lastname: Lee
authors.forename: Hyung Seop
authors.initials: HS
authors.lastname: Youn
authors.forename: Youngjin
authors.initials: Y
authors.lastname: Lee
authors.forename: Jung Youn
authors.initials: JY
authors.lastname: Kang
authors.forename: Gil Bu
authors.initials: GB
authors.lastname: Kang
authors.forename: Soo Hyun
authors.initials: SH
authors.lastname: Eom
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D019281:Dimerization; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D020124:Thermotoga maritima / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; C080466:MinC protein, Bacteria
keywords: FtsZ ring; MinC; cell division; crystal structure; domain swapping