Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-π bond.

doi:10.1107/S2053230X19007209

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Article

Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-π bond.

Acta crystallographica. Section F, Structural biology communications - 1 Jun 2019

McFarlane Jeffrey S, Ronnebaum Trey A, Meneely Kathleen M, Chilton Annemarie, Fenton Aron W, Lamb Audrey L

Abstract excerpt

Human liver pyruvate kinase (hLPYK) converts phosphoenolpyruvate to pyruvate in the final step of glycolysis. hLPYK is allosterically activated by fructose-1,6-bisphosphate (Fru-1,6-BP). The allosteric site, as defined by previous structural studies, is located in domain C between the phosphate-binding loop (residues 444-449) and the allosteric loop (residues 527-533). In this study, the X-ray crystal structures...

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Topics

Allosteric Site
Binding Sites
Cations
Crystallography, X-Ray
Fructosediphosphates

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Humans

Liver

Models, Molecular

Mutation

Protein Conformation

Protein Subunits

Pyruvate Kinase

Source

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Identifiers

PMID: 31204694
DOI: 10.1107/S2053230X19007209
PMCID: PMC6572093

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