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PMID: 11350934 Published · ppublish English Journal Article

Crystal structure of the bacterial cell division inhibitor MinC.

The EMBO journal ·Vol. 20 ·No. 10 ·2001-05-15 ·Pages 2454-61

Cordell SC, Anderson RE, Löwe J

Abstract

Bacterial cell division requires accurate selection of the middle of the cell, where the bacterial tubulin homologue FtsZ polymerizes into a ring structure. In Escherichia coli, site selection is dependent on MinC, MinD and MINE: MinC acts, with MinD, to inhibit division at sites other than the midcell by directly interacting with FTSZ: Here we report the crystal structure to 2.2 A of MinC from Thermotoga maritima. MinC consists of two domains separated by a short linker. The C-terminal domain is a right-handed beta-helix and is involved in dimer formation. The crystals contain two different MinC dimers, demonstrating flexibility in the linker region. The two-domain architecture and dimerization of MinC can be rationalized with a model of cell division inhibition. MinC does not act like SulA, which affects the GTPase activity of FtsZ, and the model can explain how MinC would select for the FtsZ polymer rather than the monomer.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/chemistry,genetics Cell Division Cloning, Molecular Crystallography, X-Ray Dimerization Genes, Bacterial Models, Molecular Molecular Sequence Data Protein Structure, Secondary Sequence Homology, Amino Acid Thermotoga maritima/chemistry,genetics
Chemicals
Bacterial Proteins MinC protein, Bacteria
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Cordell S C
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Anderson R E
Löwe J
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/20.10.2454
Published
2001-05-15
Pages
2454-61
Language
English
Region
England
NLM ID
8208664
PMCID
PMC125452
Subset
IM
External Links
PubMed source DOI: 10.1093/emboj/20.10.2454 PMC Full Text View journal details
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