5FH3
The structure of rat cytosolic PEPCK variant E89A in complex with oxalic acid and GTP
Summary for 5FH3
| Entry DOI | 10.2210/pdb5fh3/pdb |
| Related | 5FH0 5FH1 5FH2 5FH4 5FH5 |
| Descriptor | Phosphoenolpyruvate carboxykinase, cytosolic [GTP], MANGANESE (II) ION, OXALATE ION, ... (6 entities in total) |
| Functional Keywords | kinase, gluconeogenesis, lyase |
| Biological source | Rattus norvegicus (Rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 70185.69 |
| Authors | Johnson, T.A.,Holyoak, T. (deposition date: 2015-12-21, release date: 2016-11-09, Last modification date: 2023-09-27) |
| Primary citation | Johnson, T.A.,Mcleod, M.J.,Holyoak, T. Utilization of Substrate Intrinsic Binding Energy for Conformational Change and Catalytic Function in Phosphoenolpyruvate Carboxykinase. Biochemistry, 55:575-587, 2016 Cited by PubMed Abstract: Phosphoenolpyruvate carboxykinase (PEPCK) is an essential metabolic enzyme operating in the gluconeogenesis and glyceroneogenesis pathways. Previous work has demonstrated that the enzyme cycles between a catalytically inactive open state and a catalytically active closed state. The transition of the enzyme between these states requires the transition of several active site loops to shift from mobile, disordered structural elements to stable ordered states. The mechanism by which these disorder-order transitions are coupled to the ligation state of the active site however is not fully understood. To further investigate the mechanisms by which the mobility of the active site loops is coupled to enzymatic function and the transitioning of the enzyme between the two conformational states, we have conducted structural and functional studies of point mutants of E89. E89 is a proposed key member of the interaction network of mobile elements as it resides in the R-loop region of the enzyme active site. These new data demonstrate the importance of the R-loop in coordinating interactions between substrates at the OAA/PEP binding site and the mobile R- and Ω-loop domains. In turn, the studies more generally demonstrate the mechanisms by which the intrinsic ligand binding energy can be utilized in catalysis to drive unfavorable conformational changes, changes that are subsequently required for both optimal catalytic activity and fidelity. PubMed: 26709450DOI: 10.1021/acs.biochem.5b01215 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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