4MY4
Crystal structure of phosphoglycerate mutase from Staphylococcus aureus.
Summary for 4MY4
| Entry DOI | 10.2210/pdb4my4/pdb |
| Descriptor | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, MANGANESE (II) ION (3 entities in total) |
| Functional Keywords | isomerase, glycolytic enzyme, cytosol |
| Biological source | Staphylococcus aureus subsp. aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 57570.68 |
| Authors | Roychowdhury, A.,Kundu, A.,Gujar, A.,Bose, M.,Das, A.K. (deposition date: 2013-09-27, release date: 2013-10-16, Last modification date: 2023-11-08) |
| Primary citation | Roychowdhury, A.,Kundu, A.,Bose, M.,Gujar, A.,Mukherjee, S.,Das, A.K. Complete catalytic cycle of cofactor-independent phosphoglycerate mutase involves a spring-loaded mechanism Febs J., 282:1097-1110, 2015 Cited by PubMed Abstract: Cofactor-independent phosphoglycerate mutase (iPGM), an important enzyme in glycolysis and gluconeogenesis, catalyses the isomerization of 2- and 3-phosphoglycerates by an Mn(2+)-dependent phospho-transfer mechanism via a phospho-enzyme intermediate. Crystal structures of bi-domain iPGM from Staphylococcus aureus, together with substrate-bound forms, have revealed a new conformation of the enzyme, representing an intermediate state of domain movement. The substrate-binding site and the catalytic site are present in two distinct domains in the intermediate form. X-ray crystallography complemented by simulated dynamics has enabled delineation of the complete catalytic cycle, which includes binding of the substrate, followed by its positioning into the catalytic site, phospho-transfer and finally product release. The present work describes a novel mechanism of domain movement controlled by a hydrophobic patch that is exposed on domain closure and acts like a spring to keep the protein in open conformation. Domain closing occurs after substrate binding, and is essential for phospho-transfer, whereas the open conformation is a prerequisite for efficient substrate binding and product dissociation. A new model of catalysis has been proposed by correlating the hinge-bending motion with the phospho-transfer mechanism. PubMed: 25611430DOI: 10.1111/febs.13205 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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