Circular permutants in beta-glucosidases (family 3) within a predicted double-domain topology that includes a (beta/alpha)8-barrel.
By predicting the general secondary structure for beta-glucosidases (family 3), in conjunction with existing knowledge of the circular permutants present in B. fibrisolvens and R. albus, we were able to find the canonical elements of the secondary structure. The way these elements are linked suggests that there is a double-domain topology made up of a (beta/alpha)8-barrel domain and a "mainly all-beta" domain. A number of already known conserved motifs are located within (or near) the C-terminal part of the putative parallel beta-strands of the (bet/alpha)8-barrel, which is consistent with what is known about the location of catalytical sites for enzymes that have this domain topology. Within the circular permutants, two beta/alpha units are located at the N-terminal part of the molecule, whereas the other six beta/alpha units are located at the C-terminal end. In this way, the circular permutants can be seen to have a putative discontinuous double-domain topology.
García-Vallvé
S
S
University Rovira i Virgili, Department of Biochemistry and Biotechnology, Tarragona, Spain.
Rojas
A
A
Palau
J
J
Romeu
A
A
D000595:Amino Acid Sequence; D001406:Bacillaceae / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D004926:Escherichia coli; D005818:Genetic Engineering; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D013045:Species Specificity; D001617:beta-Glucosidase / Q000737:chemistry*
D001426:Bacterial Proteins; D001617:beta-Glucosidase