Format

Send to

Choose Destination
FEBS Lett. 2001 Mar 9;492(1-2):160-5.

Crystal structure of the bacterial cell division regulator MinD.

Author information

1
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. scc23@mrc-lmb.cam.ac.uk

Abstract

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.

PMID:
11248256
DOI:
10.1016/s0014-5793(01)02216-5
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center