PMID:11320321
| Citation |
Wang, S, Matsumura, P and Westbrook, EM (2001) Crystallization and preliminary X-ray crystallographic analysis of FlhD/FlhC complex from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 57:734-6 |
|---|---|
| Abstract |
The heterotetrameric (C(2)D(2)) FlhD/FlhC complex was first discovered as a transcriptional activator of the flagellar genes in Escherichia coli. Recent studies now show that FlhD/FlhC also regulates several non-flagellar target genes in E. coli. The FlhD/FlhC complex also plays several important roles in other microorganisms. The molecular interactions between FlhD and FlhC, as well as the mechanisms by which the complex may vary its DNA-binding specificity, are not clear. Determination of the FlhD/FlhC crystal structure will provide insight into these protein-protein and protein-DNA interactions. The initial steps in this investigation are reported here: the overexpression, purification and crystallization of the FlhD/FlhC complex, the characterization of this crystal form and the recording and processing of an initial diffraction data set. The obtained crystal form of the FlhD/FlhC complex is hexagonal (space group P6(1), unit-cell parameters a = b = 150.5, c = 115.9 A). The crystal density is very low (V(M) = 5.5), with 81.7% of its volume occupied by solvent. A single C(2)D(2) tetramer is present in the crystallographic asymmetric unit. A complete native data set has been collected to 4.5 A resolution. |
| Links | |
| Keywords |
Crystallization; Crystallography, X-Ray; DNA-Binding Proteins/chemistry; Electrophoresis, Polyacrylamide Gel; Escherichia coli/chemistry; Escherichia coli Proteins; Protein Conformation; Trans-Activators/chemistry |
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