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Structure of a GTP-dependent bacterial PEP-carboxykinase from Corynebacterium glutamicum.

Aich S, Prasad L, Delbaere LT
Int J Biochem Cell Biol 40 1597-603 (2008)
Cited: 5 times
EuropePMC logo PMID: 18234538

Abstract

GTP-dependent phosphoenolpyruvate carboxykinase (PCK) is the key enzyme that controls the blood glucose level during fasting in higher animals. Here we report the first substrate-free structure of a GTP-dependent phosphoenolpyruvate (PEP) carboxykinase from a bacterium, Corynebacterium glutamicum (CgPCK). The protein crystallizes in space group P2(1) with four molecules per asymmetric unit. The 2.3A resolution structure was solved by molecular replacement using the human cytosolic PCK (hcPCK) structure (PDB ID: 1KHF) as the starting model. The four molecules in the asymmetric unit pack as two dimers, and is an artifact of crystal packing. However, the P-loop and the guanine binding loop of the substrate-free CgPCK structure have different conformations from the other published GTP-specific PCK structures, which all have bound substrates and/or metal ions. It appears that a change in the P-loop and guanine binding loop conformation is necessary for substrate binding in GTP-specific PCKs, as opposed to overall domain movement in ATP-specific PCKs.

Reviews citing this publication (2)

  1. Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation. Bräsen C, Esser D, Rauch B, Siebers B. Microbiol Mol Biol Rev 78 89-175 (2014)
  2. Structural insights into the mechanism of phosphoenolpyruvate carboxykinase catalysis. Carlson GM, Holyoak T. J Biol Chem 284 27037-27041 (2009)

Articles citing this publication (3)

  1. Complex regulation of the phosphoenolpyruvate carboxykinase gene pck and characterization of its GntR-type regulator IolR as a repressor of myo-inositol utilization genes in Corynebacterium glutamicum. Klaffl S, Brocker M, Kalinowski J, Eikmanns BJ, Bott M. J Bacteriol 195 4283-4296 (2013)
  2. Electrostatic interactions play a significant role in the affinity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase for Mn2+. Sepúlveda C, Poch A, Espinoza R, Cardemil E. Biochimie 92 814-819 (2010)
  3. Stereochemistry of the carboxylation reaction catalyzed by the ATP-dependent phosphoenolpyruvate carboxykinases from Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens. Pérez E, Espinoza R, Laiveniekcs M, Cardemil E. Biochimie 90 1685-1692 (2008)


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