The N-terminal domain of VirG of Agrobacterium tumefaciens: modelling and analysis of mutant phenotypes.
Fourteen mutants in the N-terminal domain of virulence factor G (VirG) were obtained by random mutagenesis. Two mutants showed an altered phenotype, all others were non-functional. All mutants can still be phosphorylated and bind to DNA. A 3-D model was built based on the coordinates of chemotaxis protein Y (CheY). Many of the observed phenotypic changes of VirG are explained qualitatively. Combination of model building and biochemical information leads to the conclusion that the active sites of VirG and CheY must partly use different residues to perform the same phosphorylation and dephosphorylation reactions.
Institute of Molecular Plant Sciences, Leiden University, Clusius Laboratory, The Netherlands.
K W
KW
Rodenburg
E
E
Scheeren-Groot
G
G
Vriend
P J
PJ
Hooykaas
D016960:Agrobacterium tumefaciens / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003198:Computer Simulation; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D008565:Membrane Proteins / Q000737:chemistry; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D010641:Phenotype; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; C058483:virG protein, Shigella flexneri