Changes in small-angle x-ray scattering parameters observed upon binding of ligand to rabbit muscle pyruvate kinase are not correlated with allosteric transitions

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dc.contributor.authorFenton, AWen_AU
dc.contributor.authorWilliams, Ren_AU
dc.contributor.authorTrewhella, Jen_AU
dc.date.accessioned2010-09-01T04:53:31Zen_AU
dc.date.available2010-09-01T04:53:31Zen_AU
dc.date.issued2010-08-24en_AU
dc.date.statistics2010-08-24en_AU
dc.description.abstractProtein fluorescence and small-angle X-ray scattering (SAXS) have been used to monitor effector affinity and conformational changes previously associated with allosteric regulation in rabbit muscle pyruvate kinase (M-1-PYK). In the absence of substrate [phosphoenolpyruvate (PEP)], SAXS-monitored conformational changes in M-1-PYK elicited by the binding of phenylalanine (an allosteric inhibitor that reduces the affinity of M-1-PYK for PEP) are similar to those observed upon binding of alanine or 2-aminobutyric acid. Under our assay conditions, these small amino acids bind to the protein but elicit a minimal change in the affinity of the protein for PEP. Therefore, if changes in scattering signatures represent cleft closure via domain rotation as previously interpreted, we can conclude that these motions are not sufficient to elicit allosteric inhibition. Additionally, although PEP has similar affinities for the free enzyme and the M-1-PYK small amino acid complexes (i.e., the small amino acids have minimal allosteric effects), PEP binding elicits different changes in the SAXS signature of the free enzyme versus the M-1-PYK small amino acid complexes. © 2010, American Chemical Societyen_AU
dc.identifier.citationFenton, A. W., Williams, R., & Trewhella, J. (2010). Changes in small-angle x-ray scattering parameters observed upon binding of ligand to rabbit muscle pyruvate kinase are not correlated with allosteric transitions. Biochemistry, 49(33), 7202-7209. doi:10.1021/bi100147wen_AU
dc.identifier.govdoc2562en_AU
dc.identifier.issn0006-2960en_AU
dc.identifier.issue33en_AU
dc.identifier.journaltitleBiochemistryen_AU
dc.identifier.pagination7202-7209en_AU
dc.identifier.urihttp://dx.doi.org/10.1021/bi100147wen_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/2402en_AU
dc.identifier.volume49en_AU
dc.language.isoenen_AU
dc.publisherAmerican Chemical Societyen_AU
dc.subjectRabbitsen_AU
dc.subjectMusclesen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectLigandsen_AU
dc.subjectPhosphoenolpyruvateen_AU
dc.subjectAmino acidsen_AU
dc.titleChanges in small-angle x-ray scattering parameters observed upon binding of ligand to rabbit muscle pyruvate kinase are not correlated with allosteric transitionsen_AU
dc.typeJournal Articleen_AU
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