Crystal structure of the bacterial cell division regulator MinD

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.