Crystal structure of the bacterial cell division regulator MinD
Crystal structure of the bacterial cell division regulator MinD
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DOI：
10.1016/s0014-5793(01)02216-5
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发表时间：
2001-03-09
期刊：
影响因子：
3.5
通讯作者：
Löwe, J
中科院分区：
文献类型：
--
作者：
Cordell, SC;Löwe, J
在细菌细胞分裂中，MinD起着关键作用，选择中间细胞而不是其他部位。MinD与MinC形成与FtsZ相互作用的非特异性分裂抑制剂。特异性由MinD与MinE在中间细胞处的相互作用提供。我们用多重反常色散法解出了发光古生菌（Archaeoglobusfulgidus）中MinD-1的晶体结构。MinD是一种经典的核苷酸结合蛋白，与固氮酶铁蛋白相关，其具有由α-螺旋包围的七链平行β-折叠的折叠。虽然MinD，不像它与之相互作用的蛋白质和那些它在结构上相关，是一个单体，而不是二聚体，（C）2001欧洲生物化学学会联合会。由Elsevier Science B. V.出版，版权所有。
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 Angstrom 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, (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.