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Mutations close to a hub residue affect the distant active site of a GH1 β-glucosidase

التفاصيل البيبلوغرافية
العنوان: Mutations close to a hub residue affect the distant active site of a GH1 β-glucosidase
المؤلفون: Sandro R. Marana, Cecília M. Ikegami, Valquiria P. Souza, Guilherme Menegon Arantes
المصدر: PLoS ONE
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
PLoS ONE, Vol 13, Iss 6, p e0198696 (2018)
بيانات النشر: Public Library of Science, 2018.
سنة النشر: 2018
مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Cellobiose, lcsh:Medicine, medicine.disease_cause, Biochemistry, Physical Chemistry, Nitrophenols, Protein structure, Catalytic Domain, Macromolecular Structure Analysis, Centrality, Glycosides, lcsh:Science, Free Energy, Mutation, Multidisciplinary, biology, Transition (genetics), Beta-glucosidase, Chemistry, Hydrolysis, Physics, beta-Glucosidase, Chemical Reactions, Recombinant Proteins, Reaction Dynamics, Physical Sciences, Thermodynamics, Network Analysis, Research Article, Protein Structure, Computer and Information Sciences, MUTAÇÃO, Spodoptera, 03 medical and health sciences, Bacterial Proteins, medicine, Animals, Molecular Biology, Enzyme Assays, Enzyme Kinetics, Chemical Bonding, lcsh:R, Mutagenesis, Active site, Biology and Life Sciences, Proteins, Hydrogen Bonding, Transition State, biology.organism_classification, Protein tertiary structure, Protein Structure, Tertiary, Kinetics, 030104 developmental biology, Biophysics, biology.protein, Enzymology, Mutagenesis, Site-Directed, lcsh:Q, Protein Structure Networks
الوصف: The tertiary structure of proteins has been represented as a network, in which residues are nodes and their contacts are edges. Protein structure networks contain residues, called hubs or central, which are essential to form short connection pathways between any pair of nodes. Hence hub residues may effectively spread structural perturbations through the protein. To test whether modifications nearby to hub residues could affect the enzyme active site, mutations were introduced in the β-glycosidase Sfβgly (PDB-ID: 5CG0) directed to residues that form an α-helix (260-265) and a β-strand (335-337) close to one of its main hub residues, F251, which is approximately 14 Å from the Sfβgly active site. Replacement of residues A263 and A264, which side-chains project from the α-helix towards F251, decreased the rate of substrate hydrolysis. Mutation A263F was shown to weaken noncovalent interactions involved in transition state stabilization within the Sfβgly active site. Mutations placed on the opposite side of the same α-helix did not show these effects. Consistently, replacement of V336, which side-chain protrudes from a β-strand face towards F251, inactivated Sfβgly. Next to V336, mutation S337F also caused a decrease in noncovalent interactions involved in transition state stabilization. Therefore, we suggest that mutations A263F, A264F, V336F and S337F may directly perturb the position of the hub F251, which could propagate these perturbations into the Sfβgly active site through short connection pathways along the protein network.
اللغة: English
تدمد: 1932-6203
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e23e32e7c931b0adb96689dcdb9dff1d
http://europepmc.org/articles/PMC5991390
Rights: OPEN
رقم الانضمام: edsair.doi.dedup.....e23e32e7c931b0adb96689dcdb9dff1d
قاعدة البيانات: OpenAIRE
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