Structure of the apo form of Bacillus Stearothermophilus Phosphofructokinase

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dc.contributor.authorMosser, R.
dc.contributor.authorReddy, M.
dc.contributor.authorBruning, J.
dc.contributor.authorSacchettini, J.
dc.contributor.authorReinhart, G.
dc.date.issued2012
dc.description.abstractThe crystal structure of the unliganded form of Bacillus stearothermophilus phosphofructokinase (BsPFK) was determined using molecular replacement to 2.8 Å resolution (Protein Data Bank entry 3U39 ). The apo BsPFK structure serves as the basis for the interpretation of any structural changes seen in the binary or ternary complexes. When the apo BsPFK structure is compared with the previously published liganded structures of BsPFK, the structural impact that the binding of the ligands produces is revealed. This comparison shows that the apo form of BsPFK resembles the substrate-bound form of BsPFK, a finding that differs from previous predictions.
dc.description.statementofresponsibilityRockann Mosser, Manchi C. M. Reddy, John B. Bruning, James C. Sacchettini, and Gregory D. Reinhart
dc.identifier.citationBiochemistry, 2012; 51(3):769-775
dc.identifier.doi10.1021/bi201548p
dc.identifier.issn0006-2960
dc.identifier.issn1520-4995
dc.identifier.orcidBruning, J. [0000-0002-6919-1824]
dc.identifier.urihttp://hdl.handle.net/2440/76204
dc.language.isoen
dc.publisherAmer Chemical Soc
dc.rights© 2012 American Chemical Society
dc.source.urihttps://doi.org/10.1021/bi201548p
dc.subjectPhosphofructokinases
dc.subjectFructosephosphates
dc.subjectApoenzymes
dc.subjectBacterial Proteins
dc.subjectLigands
dc.subjectCrystallography, X-Ray
dc.subjectAllosteric Regulation
dc.subjectProtein Binding
dc.subjectSubstrate Specificity
dc.subjectGeobacillus stearothermophilus
dc.titleStructure of the apo form of Bacillus Stearothermophilus Phosphofructokinase
dc.typeJournal article
pubs.publication-statusPublished

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