Crystallization and preliminary X-ray crystallographic analysis of FlhD/FlhC complex from Escherichia coli

The heterotetrameric (C2D2) 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...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-05, Vol.57 (5), p.734-736
Main Authors: Wang, Shu-ying, Matsumura, Philip, Westbrook, Edwin M.
Format: Article
Language:English
Subjects:
Crystallization
Crystallography, X-Ray
DNA-Binding Proteins - chemistry
Electrophoresis, Polyacrylamide Gel
Escherichia coli - chemistry
Escherichia coli Proteins
FlhC
FlhD
Protein Conformation
Trans-Activators - chemistry
transcription factors
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Summary:The heterotetrameric (C2D2) 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 P61, unit‐cell parameters a = b = 150.5, c = 115.9 Å). The crystal density is very low (VM = 5.5), with 81.7% of its volume occupied by solvent. A single C2D2 tetramer is present in the crystallographic asymmetric unit. A complete native data set has been collected to 4.5 Å resolution.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444901003213