title: Crystal structure analysis of EstA from Arthrobacter sp. Rue61a--an insight into catalytic promiscuity.
abstract: In this article we analyze the reasons for catalytic promiscuity of a type VIII esterase with β-lactamase fold and the ability to cleave β-lactams. We compared the structure of this enzyme to those of an esterase of the same type without any lactamase ability, an esterase with moderate lactamase ability, and a class C β-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven.
authors.affiliation: Institute of Molecular Biosciences, University of Graz, A-8010 Graz, Austria. Electronic address: ulrike.wagner@uni-graz.at.
authors.forename: Ulrike Gabriella
authors.initials: UG
authors.lastname: Wagner
authors.affiliation: Biochemistry Department, University of Washington, Box 357350, Seattle, WA 98195, USA.
authors.forename: Frank
authors.initials: F
authors.lastname: DiMaio
authors.affiliation: Institute of Molecular Microbiology und Biotechnology, University of Münster, D-48149, Germany.
authors.forename: Stephan
authors.initials: S
authors.lastname: Kolkenbrock
authors.affiliation: Institute of Molecular Microbiology und Biotechnology, University of Münster, D-48149, Germany.
authors.forename: Susanne
authors.initials: S
authors.lastname: Fetzner
mesh_terms: D000595:Amino Acid Sequence; D001173:Arthrobacter / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D020134:Catalytic Domain; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D062105:Molecular Docking Simulation; D008969:Molecular Sequence Data; D010406:Penicillins / Q000737:chemistry; D011485:Protein Binding; D017433:Protein Structure, Secondary; D040681:Structural Homology, Protein; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D010406:Penicillins; D002265:Carboxylic Ester Hydrolases; C098953:EstA protein, bacteria; D001618:beta-Lactamases
keywords: Catalytic promiscuity; Crystal structure; Esterase; Steric hindrance; β-Lactamase