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Bdellovibrio bacteriovorus phosphoglucose isomerase structures reveal novel rigidity in the active site of a selected subset of enzymes upon substrate binding

DOI: 10.1098/rsob.210098 DOI Help

Authors: R. W. Meek (University of York) , I. T. Cadby (University of Birmingham) , A. L. Lovering (University of Birmingham)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Open Biology , VOL 11

State: Published (Approved)
Published: August 2021
Diamond Proposal Number(s): 10369 , 14692

Open Access Open Access

Abstract: Glycolysis and gluconeogenesis are central pathways of metabolism across all domains of life. A prominent enzyme in these pathways is phosphoglucose isomerase (PGI), which mediates the interconversion of glucose-6-phosphate and fructose-6-phosphate. The predatory bacterium Bdellovibrio bacteriovorus leads a complex life cycle, switching between intraperiplasmic replicative and extracellular ‘hunter’ attack-phase stages. Passage through this complex life cycle involves different metabolic states. Here we present the unliganded and substrate-bound structures of the B. bacteriovorus PGI, solved to 1.74 Å and 1.67 Å, respectively. These structures reveal that an induced-fit conformational change within the active site is not a prerequisite for the binding of substrates in some PGIs. Crucially, we suggest a phenylalanine residue, conserved across most PGI enzymes but substituted for glycine in B. bacteriovorus and other select organisms, is central to the induced-fit mode of substrate recognition for PGIs. This enzyme also represents the smallest conventional PGI characterized to date and probably represents the minimal requirements for a functional PGI.

Journal Keywords: Bdellovibrio bacteriovorus HD100; phosphoglucose isomerase; glucose-6-phosphate; glycolysis; fructose-6-phosphate; metabolism

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Added On: 14/08/2021 22:03


Discipline Tags:

Life Sciences & Biotech Structural biology

Technical Tags:

Diffraction Macromolecular Crystallography (MX)