7NSS
Bdellovibrio bacteriovorus PGI in P3121 spacegroup
Summary for 7NSS
| Entry DOI | 10.2210/pdb7nss/pdb |
| Descriptor | Glucose-6-phosphate isomerase, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | glucose-6-phosphate isomerase isomerase phosphoglucose isomerase, isomerase |
| Biological source | Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) |
| Total number of polymer chains | 1 |
| Total formula weight | 48117.40 |
| Authors | Meek, R.W.,Lovering, A.L. (deposition date: 2021-03-08, release date: 2021-08-18, Last modification date: 2024-01-31) |
| Primary citation | Meek, R.W.,Cadby, I.T.,Lovering, A.L. Bdellovibrio bacteriovorus phosphoglucose isomerase structures reveal novel rigidity in the active site of a selected subset of enzymes upon substrate binding. Open Biology, 11:210098-210098, 2021 Cited by PubMed 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 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 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 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. PubMed: 34375548DOI: 10.1098/rsob.210098 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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