6V2N

Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys254Ser

Replaces:  6CU4

Summary for 6V2N

• Entry DOI: 10.2210/pdb6v2n/pdb
• Descriptor: Phosphoenolpyruvate carboxykinase (ATP), CALCIUM ION, ACETATE ION, ... (4 entities in total)
• Functional Keywords: lyase, enzyme, pepcarboxykinase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 59531.85

Authors

Sokaribo, A.S.,Cotelesage, J.H.,Novakovski, B.,Goldie, H.,Sanders, D. (deposition date: 2019-11-25, release date: 2019-12-25, Last modification date: 2023-10-11)

Primary citation

Sokaribo, A.,Novakovski, B.A.A.,Cotelesage, J.,White, A.P.,Sanders, D.,Goldie, H.
Kinetic and structural analysis of Escherichia coli phosphoenolpyruvate carboxykinase mutants.
Biochim Biophys Acta Gen Subj, 1864:129517-129517, 2020

PubMed Abstract: Phosphoenolpyruvate carboxykinase (PEPCK) is a metabolic enzyme in the gluconeogenesis pathway, where it catalyzes the reversible conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) and CO. The substrates for Escherichia coli PEPCK are OAA and MgATP, with Mn acting as a cofactor. Analysis of PEPCK structures have revealed amino acid residues involved in substrate/cofactor coordination during catalysis.

PubMed: 31911238
DOI: 10.1016/j.bbagen.2020.129517

Experimental method

X-RAY DIFFRACTION (1.65 Å)