title: Structural plasticity broadens the specificity of an engineered protease.
abstract: The substrate specificity of alpha-lytic protease has been changed dramatically, with a concomitant increase in activity, by replacing an active-site Met with Ala. The substrate specificity of both this mutant and another similar mutant are extraordinarily broad. X-ray crystallographic analysis shows that structural plasticity, a combination of alternate side-chain conformations and binding-site flexibility, allows both large and small substrates to be well accommodated.
authors.affiliation: Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.
authors.forename: R
authors.initials: R
authors.lastname: Bone
authors.forename: J L
authors.initials: JL
authors.lastname: Silen
authors.forename: D A
authors.initials: DA
authors.lastname: Agard
mesh_terms: D003461:Crystallography; D015394:Molecular Structure; D009154:Mutation; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000235:genetics; D013379:Substrate Specificity
chemical_list: D012697:Serine Endopeptidases; C021826:myxobacter alpha-lytic proteinase