1FW8
CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72
Summary for 1FW8
| Entry DOI | 10.2210/pdb1fw8/pdb |
| Descriptor | Phosphoglycerate kinase, GLYCEROL (3 entities in total) |
| Functional Keywords | phosphotransferase, kinase, phosphoglycerate kinase, glycolysis, mutant, permutation, permuted sequence, pgk, protein folding, two-domain protein, transferase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Cytoplasm : P00560 |
| Total number of polymer chains | 1 |
| Total formula weight | 45022.50 |
| Authors | Tougard, P.,Bizebard, T.,Ritco-Vonsovici, M.,Minard, P.,Desmadril, M. (deposition date: 2000-09-22, release date: 2001-03-22, Last modification date: 2024-11-13) |
| Primary citation | Tougard, P.,Bizebard, T.,Ritco-Vonsovici, M.,Minard, P.,Desmadril, M. Structure of a circularly permuted phosphoglycerate kinase. Acta Crystallogr.,Sect.D, 58:2018-2023, 2002 Cited by PubMed 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. PubMed: 12454459DOI: 10.1107/S0907444902015548 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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