Crystal structure of the bacterial cell division regulator MinD |
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Authors: | Cordell S C Löwe J |
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Institution: | MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. scc23@mrc-lmb.cam.ac.uk |
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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. |
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