These months were of intense effort to revise, update and eventually submit a revised version of the FtFBPaseII manuscript to PLOS ONE. The effort centered on completing the structure solution, refinement, and analysis of two more crystal structures of FtFBPaseII that provide additional structural data to support the proposal of a new ‘framework’ for the catalytic mechanism of the entire Class II. There are now five protein structures deposited at the Protein Data Bank (PDB) associated with this paper. The accepted article was published June 23. 2023:
New structures of Class II Fructose-1,6-Bisphosphatase from Francisella tularensis provide a framework for a novel catalytic mechanism for the entire class
Selezneva AI, Harding LNM, Gutka HJ, Movahedzadeh F, Abad-Zapatero C. PLOS ONE 18(6): e0274723 [DOI]
View of the active site of FtFBPase ClassII reproduced from our PLOS ONE article.The elements of the catalysis of the cleavage of Phosphate-1 of Fructose-1,6-bis-phosphate (center green) are highlighted: i) upper right (cyan) the conserved sequence motif Arg165-Pro-Arg166 anchoring Phosphate-6 (upper right); ii) conserved motif Asp187-Gly-Asp189 (background shaded green) specifically binding the three hydroxyl groups of the furanose ring; and iii) nucleophile Thr89 and helical dipole of the two turn helix Thr89-Thr90-Ile91-Val92-Ser93-Lys94 (blue). The Mn2+ binding motif (grey) is also shown (Asp84-Pro85-Leu86-Glu87).