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
    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>

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