ArticleBiochemistry2016
Ligand Binding Enhances Millisecond Conformational Exchange in Xylanase B2 from Streptomyces lividans.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Temperature-Dependent Thumb Domain Dynamics of Xylanase TsaGH11: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Cloning, heterologus expression and characterization of a thermophilic and salt tolerant GH11 xylanase from Allostreptomyces psammosilenae YIM DR4008Antonie van Leeuwenhoek · 2025Article
- Asymmetric Dynamics Between the Protomers of the σ2 Receptor Homodimer.Journal of chemical information and modeling · 2025Article
- The PA2803-encoded PcrP exhibits a novel non-catalytic function and contributes to polymyxin B resistance inJournal of bacteriology · 2025Article
- Dynamical Signatures ofACS omega · 2025Article
- Article
- Dynamics of Ligand Binding to a Rigid Glycosidase*.Angewandte Chemie (International ed. in English) · 2020Article
- Visualizing Rev1 catalyze protein-template DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Novel xylanase producing3 Biotech · 2020Article
- AP-endonuclease 1 sculpts DNA through an anchoring tyrosine residue on the DNA intercalating loop.Nucleic acids research · 2020Article
- Nucleotide substrate binding characterization in human pancreatic-type ribonucleases.PloS one · 2019Article
- Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics.Biochemistry · 2018Article
- Modulating Enzyme Activity by Altering Protein Dynamics with Solvent.Biochemistry · 2018Article
- Why the Energy Landscape of Barnase Is Hierarchical.Frontiers in molecular biosciences · 2018Article
- Applications of NMR and computational methodologies to study protein dynamics.Archives of biochemistry and biophysics · 2017Review
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Xylanases catalyze the hydrolysis of xylan, an abundant carbon and energy source with important commercial ramifications. Despite tremendous efforts devoted to the catalytic improvement of xylanases, success remains limited because of our relatively poor understanding of their molecular properties. Previous reports suggested the potential role of atomic-scale residue dynamics in modulating the catalytic activity of GH11 xylanases; however, dynamics in these studies was probed on time scales orders of magnitude faster than the catalytic time frame. Here, we used nuclear magnetic resonance titration and relaxation dispersion experiments ((15)N-CPMG) in combination with X-ray crystallography and computational simulations to probe conformational motions occurring on the catalytically relevant millisecond time frame in xylanase B2 (XlnB2) and its catalytically impaired mutant E87A from Streptomyces lividans 66. Our results show distinct dynamical properties for the apo and ligand-bound states of the enzymes. The apo form of XlnB2 experiences conformational exchange for residues in the fingers and palm regions of the catalytic cleft, while the catalytically impaired E87A variant displays millisecond dynamics only in the fingers, demonstrating the long-range effect of the mutation on flexibility. Ligand binding induces enhanced conformational exchange of residues interacting with the ligand in the fingers and thumb loop regions, emphasizing the potential role of residue motions in the fingers and thumb loop regions for recognition, positioning, processivity, and/or stabilization of ligands in XlnB2. To the best of our knowledge, this work represents the first experimental characterization of millisecond dynamics in a GH11 xylanase family member. These results offer new insights into the potential role of conformational exchange in GH11 enzymes, providing essential dynamic information to help improve protein engineering and design applications.
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