Structures of mutants of cellulase Cel48F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action.

Parsiegla, Goetz; Reverbel, Corinne; Tardif, Chantal; Driguez, Hugues; Haser, Richard

Parsiegla, Goetz; Reverbel, Corinne; Tardif, Chantal; Driguez, Hugues; Haser, Richard.

Affiliation

Parsiegla G; Laboratoire de l'Architecture et Fonction des Macromolecules Biologiques, UMR 6098 CNRS and University of Aix-Marseille, Parc Scientifique et Technologique de Luminy, 13288 Marseille Cedex 09, France. goetz.parsiegla@afmb.univ-mrs.fr

J Mol Biol ; 375(2): 499-510, 2008 Jan 11.

Article in En | MEDLINE | ID: mdl-18035374

Subject(s)

Amino Acid Substitution; Cellulase; Clostridium cellulolyticum/enzymology; Enzyme Inhibitors/chemistry; Oligosaccharides/metabolism; Binding Sites; Carbohydrate Conformation; Cellobiose/chemistry; Cellulase/antagonists & inhibitors; Cellulase/chemistry; Cellulase/genetics; Crystallization; Crystallography, X-Ray; Glutamic Acid/metabolism; Hydrogen Bonding; Models, Chemical; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oligosaccharides/chemistry; Protein Binding; Protein Conformation; Protein Structure, Secondary; Solubility; Substrate Specificity; Thioglycosides/chemistry; Water/chemistry

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Collection: 01-internacional Database: MEDLINE Main subject: Oligosaccharides / Cellulase / Amino Acid Substitution / Clostridium cellulolyticum / Enzyme Inhibitors Language: En Journal: J Mol Biol Year: 2008 Document type: Article Affiliation country: France Country of publication: Netherlands

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