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pubmed-article:8810927pubmed:abstractTextElectron paramagnetic resonance spectroscopy at 139.5 GHz has been used to study p21 ras complexed with Mn(II) and guanosine 5'-(beta, gamma-imidotriphosphate), an analog of GTP. The p21 sample studied was selectively labeled with [17O gamma]threonine to a final enrichment of 30%. A Mn(II)-17O hyperfine interaction was observed, but the value of the coupling constant, 0.11 +/- 0.04 mT, is the smallest such value yet reported. Ab initio calculations indicate that this value is consistent with direct coordination of the threonine hydroxyl group and provide an estimate for the Mn(II)-17O bond length of 2.7 A. The measured hyperfine coupling constant and associated bond length starkly contrast with typical values for Mn(II)-17O coordination complexes, namely, approximately 0.25 mT and approximately 2.2 A, respectively. This contrast underscores the peculiar weakness of this Mn(II)-O interaction in p21 and persuasively argues that the nucleotide-induced conformational change, which is known to encompass the region of p21 involving Thr35, is not driven by Mn(II) coordination of the Thr35 hydroxyl group.lld:pubmed
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pubmed-article:8810927pubmed:articleTitleHigh frequency (139.5 GHz) electron paramagnetic resonance spectroscopy of the GTP form of p21 ras with selective 17O labeling of threonine.lld:pubmed
pubmed-article:8810927pubmed:affiliationDepartment of Biochemistry, Brandeis University, Waltham, Massachusetts 02154, USA.lld:pubmed
pubmed-article:8810927pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8810927pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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