Publication Abstract from PubMed
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.
Crystal structure of the bacterial cell division regulator MinD.,Cordell SC, Lowe J FEBS Lett. 2001 Mar 9;492(1-2):160-5. PMID:11248256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
