Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and proximity of binding sites

• Published in: PloS one Vol. 7; no. 11; p. e50488
• Main Authors: Stephen, Preyesh, Cheng, Kuo-Chang, Lyu, Ping-Chiang
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 30.11.2012; Public Library of Science (PLoS)
• Subjects: Affinity; Amylose; Amylose - metabolism; Analysis; Aspergillus awamori; Binding Sites; Biochemistry; Bioinformatics; Biology; Carbohydrates; Chemistry; Circularity; Crystal structure; Crystallography, X-Ray; Deoxyribonucleic acid; Dihydrofolate reductase; DNA; DNA shuffling; Enzymes; Glucan 1,4-alpha-Glucosidase - chemistry; Glucan 1,4-alpha-Glucosidase - genetics; Glucan 1,4-alpha-Glucosidase - metabolism; Industrial applications; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Permutations; Protein Multimerization; Protein Structure, Quaternary; Proteins; Random mutagenesis; Rhizopus - enzymology; Rhizopus oryzae; Selectivity; Site-directed mutagenesis; Spectrum analysis; Starch; Structural analysis; Structure-function relationships; Taiwan

Glucoamylases, containing starch-binding domains (SBD), have a wide range of scientific and industrial applications. Random mutagenesis and DNA shuffling of the gene encoding a starch-binding domain have resulted in only minor improvements in the affinities of the corresponding protein to their liga...