title: Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus.
abstract: The crystal structure of the major endoglucanase from the thermophilic fungus Thermoascus aurantiacus was determined by single isomorphous replacement at 1.12A resolution. The full sequence supports the classification of the protein in a subgroup of glycoside hydrolase family 5 for which no structural data are available yet. The active site shows eight critical residues, strictly conserved within family 5. In addition, aromatic residues that line the substrate-binding cleft and that are possibly involved in substrate-binding are identified. A number of residues seem to be conserved among members of the subtype, including a disulphide bridge between Cys212 and Cys249.
authors.affiliation: Laboratorium voor Eiwitbiochemie en Eiwitengineering, Universiteit Gent, B-9000, Gent, Belgium.
authors.forename: F
authors.initials: F
authors.lastname: Van Petegem
authors.forename: I
authors.initials: I
authors.lastname: Vandenberghe
authors.forename: M K
authors.initials: MK
authors.lastname: Bhat
authors.forename: J
authors.initials: J
authors.lastname: Van Beeumen
mesh_terms: D000595:Amino Acid Sequence; D001203:Ascomycota / Q000201:enzymology*; D002480:Cellulase / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid
chemical_list: D002480:Cellulase