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Organism-Adapted Specificity of the Allosteric Regulation of Pyruvate Kinase in Lactic Acid Bacteria

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SEEK ID: https://fairdomhub.org/publications/212

DOI: 10.1371/journal.pcbi.1003159

Projects: SysMO-LAB

Publication type: Not specified

Journal: PLoS Comput Biol

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Date Published: 25th Jul 2013

Registered Mode: Not specified

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Veith, N., Feldman-Salit, A., Cojocaru, V., Henrich, S., Kummer, U., & Wade, R. C. (2013). Organism-Adapted Specificity of the Allosteric Regulation of Pyruvate Kinase in Lactic Acid Bacteria. PLoS Computational Biology, 9(7), e1003159. http://doi.org/10.1371/journal.pcbi.1003159
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Created: 26th Jul 2013 at 16:34

Last updated: 26th Jul 2013 at 16:36

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Related items

Vlad Cojocaru

Projects: SysMO-LAB

Institutions: Heidelberg Institute for Theoretical Studies (HITS gGmbH)

Anna Feldman-Salit

Projects: SysMO-LAB

Institutions: Heidelberg Institute for Theoretical Studies (HITS gGmbH), University of Heidelberg

Stefan Henrich

Projects: SysMO-LAB

Institutions: Heidelberg Institute for Theoretical Studies (HITS gGmbH)

Ursula Kummer

Projects: SysMO-LAB, Kinetics on the move - Workshop 2016, de.NBI-SysBio

Institutions: University of Heidelberg

Nadine Veith

Projects: SysMO-LAB

Institutions: University of Heidelberg

Rebecca Wade

Projects: SysMO-LAB

Institutions: Heidelberg Institute for Theoretical Studies (HITS gGmbH)

SysMO-LAB

Comparative Systems Biology: Lactic Acid Bacteria

Programme: SysMO

Public web page: http://www.sysmo.net/index.php?index=57

PYK structural models
SysMO-LAB

Structural models of the LAB PYKs of L. lactis, L. plantarum, S. pyogenes and E. faecalis including the "best" docking solutions of potential allosteric ligands. The structures were derived by homology modeling based on the template of E. coli and B. stearothermophilus.
PYK models and ligands are provided as .pdb files and can be displayed by using the program PyMOL, for instance.

Creators: Nadine Veith, Anna Feldman-Salit, Stefan Henrich, Rebecca Wade

Submitter: Nadine Veith

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