Crystal structure of the bacterial cell division regulator MinD

FEBS Lett. 2001 Mar 9;492(1-2):160-5. doi: 10.1016/s0014-5793(01)02216-5.


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.

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Amino Acid Sequence
  • Archaeoglobus fulgidus / chemistry*
  • Cell Division / physiology
  • Crystallography, X-Ray
  • Escherichia coli Proteins*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Homology, Amino Acid


  • Escherichia coli Proteins
  • Adenosine Triphosphatases
  • MinD protein, E coli