Possible secondary structure in plant and yeast beta-glucanase.
Circular-dichroism spectra of a barley 1,3-beta-glucanase were analysed by two methods. The combined results predict 36-40% helix and 15-18% beta-structure in the protein. Prediction of secondary-structural features on the basis of amino acid sequence information yielded overall helix and beta-structure contents of 37% and 19% respectively. Comparison of the predicted structural elements along the barley 1,3-beta-glucanase with those of three related plant glucanases and a yeast glucanase suggest a close similarity in secondary structure among the five proteins. Consideration is given to the potential importance of certain amino acids which are conserved in these five glucanases.
MacGregor
E A
EA
Department of Chemistry, University of Manitoba, Winnipeg, Canada.
Ballance
G M
GM
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D043326:Glucan 1,3-beta-Glucosidase; D001467:Hordeum / Q000201:enzymology*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012689:Sequence Homology, Nucleic Acid; D001617:beta-Glucosidase / Q000737:chemistry* / Q000235:genetics
D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase