5xdm | pdb_00005xdm
Structure of the C-terminal domain of E. coli MinC at 3.0 angstrom resolution
Structural highlights
Function[MINC_ECOLI] Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.[1] Publication Abstract from PubMedProper cell division at the mid-site of Gram-negative bacteria reflects stringent regulation by the min system (MinC, MinD and MinE). Herein we report crystal structure of the C-terminal domain of MinC from Escherichia coli (EcMinCCTD). The MinCCTD beta helical domain is engaged in a tight homodimer, similar to Thermotoga maritima MinCCTD (TmMinCCTD). However, both EcMinCCTD and TmMinCCTD lack an alpha-helix (helix3) at their C-terminal tail, in comparison to Aquifex aerolicu MinCCTD (AaMinCCTD) which forms an extra interaction interface with MinD. To understand the role of this extra binding element in MinC/MinD interactions, we fused this helix (Aahelix3) to the C-terminus of EcMinC and examined its effect on cell morphology and cell growth. Our results revealed that Aahelix3 impaired normal cell division in vivo. Furthermore, results of a co-pelleting assay and binding free energy calculation suggested that Aahelix3 plays an essential role in AaMinCD complex formation, under the circumstance of lacking MinE in A. aerolicu. Combining these results with sequence analysis of MinC and MinD in different organisms, we propose an evolutionary relationship to rationalize different mechanisms in cell division positioning in various organisms. Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division.,Yang S, Shen Q, Wang S, Song C, Lei Z, Han S, Zhang X, Zheng J, Jia Z Sci Rep. 2017 Aug 8;7(1):7627. doi: 10.1038/s41598-017-08213-5. PMID:28790446[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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