Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations. - Wikidata - awgldk - TriplyDB

Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.

Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.

http://www.wikidata.org/entity/Q33223608

about

The molecular basis of glyphosate resistance by an optimized microbial acetyltransferase Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility Biocatalytic and structural properties of a highly engineered halohydrin dehalogenase Plastid localization of the key carotenoid enzyme phytoene synthase is altered by isozyme, allelic variation, and activity.Fisher's geometric model of adaptation meets the functional synthesis: data on pairwise epistasis for fitness yields insights into the shape and size of phenotype space Evolution of broad spectrum β-lactam resistance in an engineered metallo-β-lactamase.How protein stability and new functions trade off The role of a second-shell residue in modifying substrate and inhibitor interactions in the SHV beta-lactamase: a study of ambler position Asn276.Single-mutation fitness landscapes for an enzyme on multiple substrates reveal specificity is globally encoded Active site detection by spatial conformity and electrostatic analysis--unravelling a proteolytic function in shrimp alkaline phosphatase.NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices.A combined molecular dynamics and rapid kinetics approach to identify conserved three-dimensional communication networks in elongation factor Tu Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.How structural and physicochemical determinants shape sequence constraints in a functional enzyme Investigation of Structural Determinants for the Substrate Specificity in the Zinc-Dependent Alcohol Dehydrogenase CPCR2 from Candida parapsilosis.Meropenem and chromacef intermediates observed in IMP-25 metallo-β-lactamase-catalyzed hydrolysis.Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus.Biochemical characterization of metallo-beta-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strain.B1-Metallo-β-Lactamases: Where Do We Stand?IND-6, a highly divergent IND-type metallo-beta-lactamase from Chryseobacterium indologenes strain 597 isolated in Burkina Faso.Insights into an evolutionary strategy leading to antibiotic resistance.Metallo-β-lactamase structure and function.A variety of roles for versatile zinc in metallo-β-lactamases.Prediction of distal residue participation in enzyme catalysis.Danger lurking in the "unknowns": structure-to-function studies of hypothetical protein Bleg1_2437 from Bacillus lehensis G1 alkaliphile revealed an evolutionary divergent B3 metallo-beta-lactamase.Exploring the conformational and reactive dynamics of biomolecules in solution using an extended version of the glycine reactive force field.Allosteric inhibition of VIM metallo-β-lactamases by a camelid nanobody.Hydrolysis of cephalexin and meropenem by New Delhi metallo-β-lactamase: the substrate protonation mechanism is drug dependent.Optimization of Conformational Dynamics in an Epistatic Evolutionary Trajectory.On the active site of mononuclear B1 metallo β-lactamases: a computational study

P2860

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P2860

Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.

http://www.wikidata.org/entity/Q33223608

description

2005 nî lūn-bûn

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2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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Alejandro J Vila

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Pablo E Tomatis

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Rodolfo M Rasia

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P2860

DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold

Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor

Predicting the emergence of antibiotic resistance by directed evolution and structural analysis

Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase

The structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34

Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs

Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril

The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril

Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis

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102

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