Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Cordell SC, Lowe J. Crystal structure of the bacterial cell division regulator MinD. FEBS Lett. 2001 Mar 9;492(1-2):160-5. PMID:11248256
