Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis.
The inter- and intramolecular interactions between the different domains of the catalase-peroxidase KatG from Mycobacterium tuberculosis were analyzed using the two-hybrid assay. It was shown that the dimerization of the enzyme is due to a strong interaction of the first 99 amino acids of the N-terminal domain whereas the C-terminal domain does not play a role in the dimerization. In addition, an intramolecular interaction between the N- and C-terminal domains was detected which might play a functional role in the mechanism of the enzyme.
Wilming
M
M
Institute of Organic Chemistry, Swiss Federal Institute of Technology, Lausanne, Switzerland
Johnsson
K
K
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001665:Binding Sites; D019281:Dimerization; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000201:enzymology* / Q000235:genetics; D010544:Peroxidases / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases; D020798:Two-Hybrid System Techniques; D000099160:LexA Repressor Protein
D001426:Bacterial Proteins; D010544:Peroxidases; D011993:Recombinant Fusion Proteins; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein; C076136:catalase HPI