7ntg

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Bdellovibrio bacteriovorus PGI in complex with fructose-6-phosphateBdellovibrio bacteriovorus PGI in complex with fructose-6-phosphate

Structural highlights

7ntg is a 1 chain structure with sequence from Bdellovibrio bacteriovorus HD100. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.67Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6MPU9_BDEBA

Publication Abstract from PubMed

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 A and 1.67 A, 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.

Bdellovibrio bacteriovorus phosphoglucose isomerase structures reveal novel rigidity in the active site of a selected subset of enzymes upon substrate binding.,Meek RW, Cadby IT, Lovering AL Open Biol. 2021 Aug;11(8):210098. doi: 10.1098/rsob.210098. Epub 2021 Aug 11. PMID:34375548[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Meek RW, Cadby IT, Lovering AL. Bdellovibrio bacteriovorus phosphoglucose isomerase structures reveal novel rigidity in the active site of a selected subset of enzymes upon substrate binding. Open Biol. 2021 Aug;11(8):210098. doi: 10.1098/rsob.210098. Epub 2021 Aug 11. PMID:34375548 doi:http://dx.doi.org/10.1098/rsob.210098

7ntg, resolution 1.67Å

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OCA