Cordell S C, Löwe J
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
FEBS Lett. 2001 Mar 9;492(1-2):160-5. doi: 10.1016/s0014-5793(01)02216-5.
In bacterial cell division MinD plays a pivotal role, selecting the mid-cell over other sites. With MinC, MinD forms a non-specific inhibitor of division, that interacts with FtsZ. Specificity is provided by MinD's interaction with MinE at the mid-cell. We have solved the crystal structure of MinD-1 from Archaeoglobus fulgidus to 2.6 A by multiple anomalous dispersion. MinD is a classic nucleotide binding protein, related to nitrogenase iron proteins, which have a fold of a seven-stranded parallel beta-sheet, surrounded by alpha-helices. Although MinD, unlike the proteins it interacts with and those it is structurally related to, is a monomer, not a dimer.
在细菌细胞分裂过程中，MinD起着关键作用，它能在细胞中部而非其他位点进行选择。MinD与MinC一起形成一种非特异性的分裂抑制剂，该抑制剂与FtsZ相互作用。细胞中部MinD与MinE的相互作用赋予了其特异性。我们通过多波长反常散射法解析了来自嗜热栖热菌的MinD-1的晶体结构，分辨率达到2.6埃。MinD是一种典型的核苷酸结合蛋白，与固氮酶铁蛋白相关，其具有由α螺旋包围的七股平行β折叠结构。尽管与它相互作用的蛋白质以及在结构上与之相关的蛋白质不同，MinD是单体而非二聚体。
