Anatomy of a conformational change: Hinged 'lid' motion of the triosephosphate isomerase loop Academic Article uri icon

Overview

MeSH Major

  • Carbohydrate Epimerases
  • Protein Conformation
  • Triose-Phosphate Isomerase

abstract

  • Triosephosphate isomerase (TIM) is used as a model system for the study of how a localized conformational change in a protein structure is produced and related to enzyme reactivity. An 11-residue loop region moves more than 7 angstroms and closes over the active site when substrate binds. The loop acts like a "lid" in that it moves rigidly and is attached by two hinges to the remainder of the protein. The nature of the motion appears to be built into the loop by conserved residues; the hinge regions, in contrast, are not conserved. Results of molecular dynamics calculations confirm the structural analysis and suggest a possible ligand-induced mechanism for loop closure.

publication date

  • October 19, 1990

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed ID

  • 2402636

Additional Document Info

start page

  • 1425

end page

  • 8

volume

  • 249

number

  • 4975