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 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.
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. scc23@mrc-lmb.cam.ac.uk
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D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000595:Amino Acid Sequence; D019611:Archaeoglobus fulgidus / Q000737:chemistry*; D002455:Cell Division / Q000502:physiology; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D029968:Escherichia coli Proteins; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli