Crystal structure of the bacterial cell division regulator MinD

FEBS Letters

Löwe, Jan¹  Cordell, Suzanne C¹ 

[1] MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK

关键词: Cell division;    Crystal structure;    MinD;    MinC;    FtsZ;   

DOI  :  10.1016/S0014-5793(01)02216-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Å 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 β-sheet, surrounded by α-helices. Although MinD, unlike the proteins it interacts with and those it is structurally related to, is a monomer, not a dimer.

【 授权许可】

Unknown