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Backbone Assignment of a 28.5 kDa Class A Extended Spectrum β-Lactamase by High-Field, Carbon-Detected Solid-State NMR

Williams, C. G.; Wang, S.; Thome, A. F.; Warmuth, O. A.; Sakhrani, V.; Rienstra, C. M.; Mueller, L. J.

2025-05-19 biochemistry
10.1101/2025.05.18.654753 bioRxiv
Show abstract

13C and 15N backbone chemical shift assignments are reported for the 28.5 kDa protein Toho-1 {beta}-lactamase, a Class A extended spectrum {beta}-lactamase. A very high level of assignment completeness (97% of the backbone) is enabled by the combined sensitivity and resolution gains of ultrahigh-field NMR spectroscopy (1.1 GHz), improved probe technology, and optimized pulse sequences. The assigned chemical shifts agree well with our previous solution-state NMR assignments, indicating that the secondary structure is conserved in the solid state. These assignments provide a foundation for future investigations of sidechain chemical shifts and catalytic mechanism.

Published in Biomolecular NMR Assignments · not in our set (fewer than 10 published preprints to learn from) · training set

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