PMID:11248256
| Citation |
Cordell, SC and Löwe, J (2001) Crystal structure of the bacterial cell division regulator MinD. FEBS Lett. 492:160-5 |
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| Abstract |
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. |
| Links | |
| Keywords |
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 |
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