Structural and biochemical characterization of the class II fructose-1,6-bisphosphatase from Francisella tularensis.

ABSTRACT: The crystal structure of the class II fructose-1,6-bisphosphatase (FBPaseII) from the important pathogen Francisella tularensis is presented at 2.4 Å resolution. Its structural and functional relationships to the closely related phosphatases from Mycobacterium tuberculosis (MtFBPaseII) and Escherichia coli (EcFBPaseII) and to the dual phosphatase from Synechocystis strain 6803 are discussed. FBPaseII from F. tularensis (FtFBPaseII) was crystallized in a monoclinic crystal form (space group P2₁, unit-cell parameters a = 76.30, b = 100.17, c = 92.02 Å, β = 90.003°) with four chains in the asymmetric unit. Chain A had two coordinated Mg²⁺ ions in its active center, which is distinct from previous findings, and is presumably deactivated by their presence. The structure re

SUBMITTER: Selezneva AI 

PROVIDER: S-EPMC7605111 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature