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Structure of a circularly permuted phosphoglycerate kinase
Pierre Tougard1, Thierry Bizebard, Monica Ritco-Vonsovici
1Laboratoire de Modélisation et d'Ingénierie des Protéines, UMR 8619, Université de Paris-Sud, Bâtiment 430, F-91405 Orsay CEDEX, France.
Acta Crystallographica. Section D, Biological Crystallography
|November 28, 2002
Summary
Circularly permuted yeast phosphoglycerate kinase (72p yPGK) structure reveals protein folding continuity is not essential. Limited structural changes were observed, impacting hinge-bending motion and protein function.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Engineering
Background:
- Yeast phosphoglycerate kinase (PGK) is a crucial enzyme in glycolysis.
- Understanding protein folding mechanisms is fundamental in biochemistry.
- Circular permutation offers insights into protein structural stability and function.
Purpose of the Study:
- To determine the crystallographic structure of a circularly permuted yeast PGK (72p yPGK).
- To investigate the impact of circular permutation on protein structure and folding.
- To elucidate the relationship between protein structure and functional properties.
Main Methods:
- X-ray crystallography
- Molecular replacement
- Protein engineering
Main Results:
- The 2.3 A resolution structure of 72p yPGK was determined.
- The overall fold is similar to wild-type PGK, indicating folding continuity is not essential.
- Limited structural changes were observed near the new peptide bond and in flexible loops.
- The permuted protein exhibits an open/twisted domain conformation.
- Functional effects are attributed to restricted hinge-bending motion.
Conclusions:
- Protein folding does not strictly require the continuity of a folding unit.
- Circular permutation can alter protein conformation and dynamics.
- Structural changes in 72p yPGK affect hinge-bending motion, influencing enzyme function.