title: Structure of a circularly permuted phosphoglycerate kinase.
abstract: The crystallographic structure of a circularly permuted form of yeast PGK, 72p yPGK, has been determined to a resolution of 2.3 A by molecular replacement. In this engineered protein, the C- and N-terminal residues of the wild-type protein are directly connected by a peptide bond and new N- and C-terminal residues are located within the N-terminal domain. The overall fold of the protein is very similar to that of the wild-type protein, directly demonstrating that the continuity of a folding unit is not relevant to the folding process of the whole protein. Only limited structural changes were observed: these were in the regions associated with the new connection, in a long flexible loop in the permuted domain and in the vicinity of Arg38, a functionally important residue. The relative positions of the two domains suggested that this permuted protein adopts one of the most open/twisted conformations seen amongst PGKs of known structure. The effect of the mutation on the functional properties is more easily accounted for by a restriction of hinge-bending motion than by structural changes in the protein.
authors.affiliation: Laboratoire de Modélisation et d'Ingénierie des Protéines, UMR 8619, Université de Paris-Sud, Bâtiment 430, F-91405 Orsay CEDEX, France.
authors.forename: Pierre
authors.initials: P
authors.lastname: Tougard
authors.forename: Thierry
authors.initials: T
authors.lastname: Bizebard
authors.forename: Monica
authors.initials: M
authors.lastname: Ritco-Vonsovici
authors.forename: Philippe
authors.initials: P
authors.lastname: Minard
authors.forename: Michel
authors.initials: M
authors.lastname: Desmadril
mesh_terms: D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010735:Phosphoglycerate Kinase / Q000737:chemistry*; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology
chemical_list: D010735:Phosphoglycerate Kinase