7O0A

Bdellovibrio bacteriovorus PGI in P1211 spacegroup

7O0A の概要

• エントリーDOI: 10.2210/pdb7o0a/pdb
• 関連するPDBエントリー: 7NSS 7NTG
• 分子名称: Glucose-6-phosphate isomerase, 1,2-ETHANEDIOL, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: pgi, phosphoglucose isomerase, gpi, glucose-6-phosphate isomerase, isomerase
• 由来する生物種: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 384803.00

構造登録者

Meek, R.W.,Lovering, A.L. (登録日: 2021-03-26, 公開日: 2021-08-18, 最終更新日: 2024-01-31)

主引用文献

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

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: 34375548
DOI: 10.1098/rsob.210098

実験手法

X-RAY DIFFRACTION (1.74 Å)