Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. Academic Article uri icon

Overview

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

  • September 21, 1990

Research

keywords

  • Carbohydrate Epimerases
  • Protein Conformation
  • Triose-Phosphate Isomerase

Identity

Scopus Document Identifier

  • 0025015392

PubMed ID

  • 2402636

Additional Document Info

volume

  • 249

issue

  • 4975