4L1C

Crystal structure of Dimerized N-terminal Domain of MinC

4L1C の概要

• エントリーDOI: 10.2210/pdb4l1c/pdb
• 分子名称: Probable septum site-determining protein MinC (2 entities in total)
• 機能のキーワード: swapping, antiparallel beta sheet, cell division inhibitor, ftsz, protein binding
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21693.15

構造登録者

An, J.Y.,Kim, T.G.,Park, K.R.,Lee, J.G.,Youn, H.S.,Kang, J.Y.,Lee, Y.,Kang, G.B.,Eom, S.H. (登録日: 2013-06-03, 公開日: 2013-10-23, 最終更新日: 2024-02-28)

主引用文献

An, J.Y.,Kim, T.G.,Park, K.R.,Lee, J.G.,Youn, H.S.,Lee, Y.,Kang, J.Y.,Kang, G.B.,Eom, S.H.
Crystal structure of the N-terminal domain of MinC dimerized via domain swapping.
J Synchrotron Radiat, 20:984-988, 2013

PubMed 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.

PubMed: 24121353
DOI: 10.1107/S0909049513022760

実験手法

X-RAY DIFFRACTION (2.28 Å)