Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional 1H-detected solid-state NMR

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dc.contributor.authorKlein, Alexander
dc.contributor.authorRovó, Petra
dc.contributor.authorSakhrani, Varun V.
dc.contributor.authorWang, Yangyang
dc.contributor.authorHolmes, Jacob B.
dc.contributor.authorLiu, Viktoriia
dc.contributor.authorSkowronek, Patricia
dc.contributor.authorKukuk, Laura
dc.contributor.authorVasa, Suresh K.
dc.contributor.authorGüntert, Peter
dc.contributor.authorMueller, Leonard J.
dc.contributor.authorLinser, Rasmus
dc.date.accessioned2026-01-15T07:46:46Z
dc.date.available2026-01-15T07:46:46Z
dc.date.issued2022-01-20
dc.description.abstractNMR chemical shifts provide detailed information on the chemical properties of molecules, thereby complementing structural data from techniques like X-ray crystallography and electron microscopy. Detailed analysis of protein NMR data, however, often hinges on comprehensive, site-specific assignment of backbone resonances, which becomes a bottleneck for molecular weights beyond 40 to 45 kDa. Here, we show that assignments for the (2x)72-kDa protein tryptophan synthase (665 amino acids per asymmetric unit) can be achieved via higher-dimensional, proton-detected, solid-state NMR using a single, 1-mg, uniformly labeled, microcrystalline sample. This framework grants access to atom-specific characterization of chemical properties and relaxation for the backbone and side chains, including those residues important for the catalytic turnover. Combined with first-principles calculations, the chemical shifts in the β-subunit active site suggest a connection between active-site chemistry, the electrostatic environment, and catalytically important dynamics of the portal to the β-subunit from solution.en
dc.identifier.urihttp://hdl.handle.net/2003/44667
dc.language.isoen
dc.relation.ispartofseriesProceedings of the National Academy of Sciences of the United States of America; 119(4)
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectSolid-state NMRen
dc.subjectNMR crystallographyen
dc.subjectTryptophan synthaseen
dc.subjectPLP- dependent enzymesen
dc.subjectTautomerismen
dc.subject.ddc540
dc.subject.rswkFestkörper-NMR-Spektroskopie
dc.subject.rswkPyridoxalphosphat
dc.subject.rswkEnzym
dc.subject.rswkSynthasen
dc.subject.rswkTryptophan
dc.subject.rswkTautomerie
dc.titleAtomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional 1H-detected solid-state NMRen
dc.typeText
dc.type.publicationtypeResearchArticle
dcterms.accessRightsopen access
eldorado.dnb.deposittrue
eldorado.doi.registerfalse
eldorado.secondarypublicationtrue
eldorado.secondarypublication.primarycitationKlein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J., & Linser, R. (2022). Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional 1H-detected solid-state NMR. Proceedings of the National Academy of Sciences of the United States of America, 119(4), Article e2114690119. https://doi.org/10.1073/pnas.2114690119
eldorado.secondarypublication.primaryidentifierhttps://doi.org/10.1073/pnas.2114690119

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Fakultät für Chemie und Chemische Biologie