Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Conformational changes observed in enzyme crystal structures upon substrate binding.

Alex Gutteridge1, Janet Thornton

  • 1European Bioinformatics Institute, EMBL Outstation-Hinxton, Wellcome Trust Genome Campus, CB10 1SD Hinxton Cambridge, UK. alexg@ebi.ac.uk

Journal of Molecular Biology
|January 25, 2005
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Analysis of FAIMS for the study of affinity-purified protein complexes using the orbitrap ascend tribrid mass spectrometer.

Molecular omics·2025
Same author

Lineage-specific patterns in the Moraceae family allow identification of convergent P450 enzymes involved in furanocoumarin biosynthesis.

The New phytologist·2025
Same author

Analysis of FAIMS for the Study of Affinity-Purified Protein Complexes Using the Orbitrap Ascend Tribrid Mass Spectrometer.

bioRxiv : the preprint server for biology·2024
Same author

Distinct Regions within SAP25 Recruit O-Linked Glycosylation, DNA Demethylation, and Ubiquitin Ligase and Hydrolase Activities to the Sin3/HDAC Complex.

Journal of proteome research·2024
Same author

Causal inference can lead us to modifiable mechanisms and informative archetypes in sepsis.

Intensive care medicine·2024
Same author

Distinct regions within SAP25 recruit O-linked glycosylation, DNA demethylation, and ubiquitin ligase and hydrolase activities to the Sin3/HDAC complex.

bioRxiv : the preprint server for biology·2024
Same journal

UPF3A and UPF3B shape the transcriptome cooperatively yet oppose cell function.

Journal of molecular biology·2026
Same journal

Antibody-secreting cells integrate efficient NMD with non‑canonical UPR signaling to maintain proteostasis and support massive immunoglobulin synthesis.

Journal of molecular biology·2026
Same journal

Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry.

Journal of molecular biology·2026
Same journal

UPF1 at Work: Structural and Mechanistic Insights Into a Master Regulator of Nonsense-Mediated mRNA Decay.

Journal of molecular biology·2026
Same journal

Structural basis for the pro-amyloidogenic action and ligand binding of a novel W72R variant of human apolipoprotein A-I.

Journal of molecular biology·2026
Same journal

Cryo-EM Structure of the C. elegans Septin Tetramer Reveals a Revised Architecture and Conserved Positional Orthology.

Journal of molecular biology·2026
See all related articles

Enzyme conformational changes upon substrate binding, known as induced fit, are often minimal. Analysis of 60 enzymes reveals small protein-wide motions but significant side-chain flexibility in both binding and catalytic residues.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • The induced fit theory posits enzymes change conformation upon substrate binding.
  • Understanding these conformational changes is key to enzyme function.

Purpose of the Study:

  • To investigate the extent of conformational changes in enzymes between apo and substrate-bound states.
  • To analyze how these changes affect active site residues involved in binding and catalysis.

Main Methods:

  • Structural analysis of 60 different enzymes.
  • Comparison of apo and substrate-bound forms.
  • Examination of catalytic and substrate-binding residues.

Main Results:

  • Induced fit motions are generally small, with ~1 Å RMSD across the whole protein.

Related Experiment Videos

  • Binding residues exhibit larger backbone motions than catalytic residues.
  • Both binding and catalytic residues display substantial side-chain flexibility.

    • Conclusions:

    • Enzyme conformational changes upon substrate binding are subtle.
    • Differential flexibility exists between binding and catalytic residues.
    • Quantifying induced fit aids understanding of enzyme catalysis and improves ligand docking strategies.