Crystal structure of the bacterial cell division regulator MinD

被引：69

作者：

Cordell, SC ^{[1
]}

Löwe, J ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

来源：

FEBS LETTERS | 2001年 / 492卷 / 1-2期

关键词：

cell division; crystal structure; MinD; MinC; FtsZ;

D O I：

10.1016/S0014-5793(01)02216-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 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.

引用

页码：160 / +

页数：7

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