Interspecies hybrid tryptophan synthase-modified beta 2 protein formed from separate folding regions of the beta monomer.
Escherichia coli and Serratia marcescens tryptophan synthase beta 2 protein (EC 4.2.1.20) was subjected to mild trypsin proteolysis. Two separate folding regions (domains) of the E. coli (EF1 and EF2) and the S. marcescens (SF1 and SF2) enzyme were shown to form interspecies hybrid reconstituted molecules [(EF1-SF2)2 and (SF1-EF2)2] and intraspecies reconstituted molecules [(EF1-EF2)2 and (SF1-SF2)2] with equal efficiency. The data suggest that structural regions, associated with beta monomer assembly, exist somewhere on the domain fragments and that these regions are conserved.
D001426:Bacterial Proteins; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D012706:Serratia marcescens / Q000201:enzymology*; D013045:Species Specificity; D014357:Trypsin / Q000494:pharmacology; D014367:Tryptophan Synthase / Q000378:metabolism
D001426:Bacterial Proteins; D014357:Trypsin; D014367:Tryptophan Synthase