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

Alexander Klein, Petra Rovó, Varun V. Sakhrani, Yangyang Wang, Jacob B. Holmes, Viktoriia Liu, Patricia Skowronek, Laura Kukuk, Suresh K. Vasa, Peter Güntert, Leonard J. Mueller, Rasmus Linser

doi:10.1073/pnas.2114690119

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

DOI Web Site Web Site 88 References Open Access

Alexander Klein

Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany
Petra Rovó

Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany
Varun V. Sakhrani

Department of Chemistry, University of California, Riverside, CA 92521
Yangyang Wang

Department of Chemistry, University of California, Riverside, CA 92521
Jacob B. Holmes

Department of Chemistry, University of California, Riverside, CA 92521
Viktoriia Liu

Department of Chemistry, University of California, Riverside, CA 92521
Patricia Skowronek

Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany
Laura Kukuk

Department of Chemistry and Chemical Biology, TU Dortmund University, 44227 Dortmund, Germany
Suresh K. Vasa

Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany
Peter Güntert

Institute of Biophysical Chemistry, Goethe University, 60438 Frankfurt am Main, Germany
Leonard J. Mueller

Department of Chemistry, University of California, Riverside, CA 92521
Rasmus Linser

Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany

Abstract

<jats:title>Significance</jats:title> <jats:p>The atomic-level understanding of protein function and enzyme catalysis requires site-specific information on chemical properties such as protonation and hybridization states and chemical exchange equilibria. This information is encoded in NMR chemical shifts, which serve as important complementary information to structural data from other experimental techniques or structure prediction algorithms. This study demonstrates that comprehensive chemical-shift assignments are achievable for large and highly complex proteins, offering insights into chemical structure and dynamics. The access to the active-site chemistry in the 144-kDa (72-kDa asymmetric unit) enzyme tryptophan synthase demonstrated here extends the elucidation of chemical properties to a member of an important class of enzymes of interest in pharmacology and biotechnology.</jats:p>

Journal

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences 119 (4), 2022-01-20

Proceedings of the National Academy of Sciences

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