The role of conserved tryptophan residues in the interaction of a bacterial cellulose binding domain with its ligand
作者： Debbie M. Poole , Geoffrey P. Hazlewood , Neville S. Huskisson , Richard Virden , Harry J. Gilbert
DOI: 10.1111/J.1574-6968.1993.TB05938.X
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摘要: The five conserved tryptophan residues in the cellulose binding domain of xylanase A from Pseudomonas fluorescens subsp. cellulosa were replaced with alanine and phenylalanine. mutated domains fused to mature alkaline phosphatase, capacity hybrid proteins bind was assessed. Alanine substitution residues, general, resulted a significant decrease cellulose. Mutant containing phenylalanine retained some affinity for C-terminal proximal did not play an important role ligand binding, while Trp13, Trp34 Trp38 essential retain capacity. Data presented this study suggest major differences mechanism attachment between Cellulomonas domains.
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