Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

PloS one - 1 Jan 2018

Souza Valquiria P, Ikegami Cecília M, Arantes Guilherme M, Marana Sandro R

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to beta-Glucosidase
Share to Catalytic Domain
Share to Enzyme Assays

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosides

Share to Hydrolysis

Share to Mutagenesis, Site-Directed

Share to Nitrophenols

Share to Spodoptera

Source

Open in PubMed Open full text

Identifiers

PMID: 29874288
DOI: 10.1371/journal.pone.0198696
PMCID: PMC5991390

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations close to a hub residue affect the distant active site of a GH1 β-glucosidase.PMID 29874288Read ↗

Dynamic coupling of residues within proteins as a mechanistic foundation of many enigmatic pathogenic missense variants.Semantic proximity Read ↗

Free energy-guided Q302P mutation in GH1 β-glucosidase from Aspergillus fumigatus improves enzyme function via catalytic tunnel perturbation.Semantic proximity Read ↗

Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.Semantic proximity Read ↗

Glutantβase: a database for improving the rational design of glucose-tolerant β-glucosidases.Semantic proximity Read ↗

Glucose 6-phosphate dehydrogenase mutations causing enzyme deficiency in a model of the tertiary structure of the human enzymeSemantic proximity Read ↗

Effects of Distal Mutations on Prolyl-Adenylate Formation of Escherichia coli Prolyl-tRNA Synthetase.Semantic proximity Read ↗

Distal mutation V486M disrupts the catalytic activity of DPP4 by affecting the flap of the propeller domain.Semantic proximity Read ↗

Single mutations of residues outside the active center of the xylanase Xys1 Delta from Streptomyces halstedii JM8 affect its activity.Semantic proximity Read ↗

Harvesting the high-hanging fruit: the structure of the YdeN gene product from Bacillus subtilis at 1.8 angstroms resolution.Semantic proximity Read ↗

Identification of furin pro-region determinants involved in folding and activation.Semantic proximity Read ↗

Structural insights reveal the second base catalyst of isomaltose glucohydrolase.Semantic proximity Read ↗

Understanding the role of histidine in the GHSxG acyltransferase active site motif: evidence for histidine stabilization of the malonyl-enzyme intermediate.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.