5XDM

Structure of the C-terminal domain of E. coli MinC at 3.0 angstrom resolution

5XDM の概要

• エントリーDOI: 10.2210/pdb5xdm/pdb
• 分子名称: Septum site-determining protein MinC (1 entity in total)
• 機能のキーワード: cell division inhibition, dimer, p4322, beta helical, cell cycle
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26257.79

構造登録者

Zheng, J.,Shen, Q.,Yang, S. (登録日: 2017-03-28, 公開日: 2018-02-07, 最終更新日: 2023-11-22)

主引用文献

Yang, S.,Shen, Q.,Wang, S.,Song, C.,Lei, Z.,Han, S.,Zhang, X.,Zheng, J.,Jia, Z.
Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division
Sci Rep, 7:7627-7627, 2017

PubMed Abstract: Proper 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 (EcMinC). The MinC beta helical domain is engaged in a tight homodimer, similar to Thermotoga maritima MinC (TmMinC). However, both EcMinC and TmMinC lack an α-helix (helix3) at their C-terminal tail, in comparison to Aquifex aerolicu MinC (AaMinC) 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.

PubMed: 28790446
DOI: 10.1038/s41598-017-08213-5

実験手法

X-RAY DIFFRACTION (3.004 Å)