Williams Christopher G, Wang Songlin, Thome Alexander F, Warmuth Owen A, Sakhrani Varun, Rienstra Chad M, Mueller Leonard J
Department of Chemistry, University of California, Riverside, Riverside, CA 92521, USA.
Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
bioRxiv. 2025 May 19:2025.05.18.654753. doi: 10.1101/2025.05.18.654753.
C and N backbone chemical shift assignments are reported for the 28.5 kDa protein Toho-1 β-lactamase, a Class A extended spectrum β-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.
已报道了28.5 kDa的东和-1β-内酰胺酶（一种A类超广谱β-内酰胺酶）的碳（C）和氮（N）主链化学位移归属。超高场核磁共振波谱（1.1 GHz）、改进的探头技术和优化的脉冲序列相结合带来的灵敏度和分辨率提升，使得主链归属的完整性达到了很高的水平（97%）。所归属的化学位移与我们之前在溶液状态下的核磁共振归属结果吻合良好，表明二级结构在固态中得以保留。这些归属为未来侧链化学位移和催化机制的研究奠定了基础。
