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1H, 13C, and 15N resonance assignments of Fusarium solani pisi cutinase and preliminary features of the structure in solution

Essentially complete (96%) sequence‐specific assignments were made for the backbone and side‐chain 1H, 13C, and 15N resonances of Fusarium solani pisi cutinase, produced as a 214‐residue heterologous protein in Escherichia coli, using heteronuclear NMR techniques. Three structural features were noticed during the assignment. (1) The secondary structure in solution corresponds mostly with the structure from X‐ray diffraction, suggesting that both structures are globally similar. (2) The HN of Ala32 has a strongly upfield‐shifted resonance at 3.97 ppm, indicative of an amide‐aromatic hydrogen bond to the indole ring of Trp69 that stabilizes the N‐terminal side of the parallel β‐sheet. (3) The NMR data suggest that the residues constituting the oxyanion hole are quite mobile in the free enzyme in solution, in contrast to the existence of a preformed oxyanion hole as observed in the crystal structure. Apparently, cutinase forms its oxyanion hole upon binding of the substrate like true lipases.