6R5I

The crystal structure of the Glycoside Hydrolase BglX from P. aeruginosa

6R5I の概要

• エントリーDOI: 10.2210/pdb6r5i/pdb
• 分子名称: Periplasmic beta-glucosidase, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: glycoside hydrolase, hydrolase
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 160648.58

構造登録者

Batuecas, M.T.,Hermoso, J.A. (登録日: 2019-03-25, 公開日: 2020-04-15, 最終更新日: 2024-01-24)

主引用文献

Mahasenan, K.V.,Batuecas, M.T.,De Benedetti, S.,Kim, C.,Rana, N.,Lee, M.,Hesek, D.,Fisher, J.F.,Sanz-Aparicio, J.,Hermoso, J.A.,Mobashery, S.
Catalytic Cycle of Glycoside Hydrolase BglX fromPseudomonas aeruginosaand Its Implications for Biofilm Formation.
Acs Chem.Biol., 15:189-196, 2020

PubMed Abstract: BglX is a heretofore uncharacterized periplasmic glycoside hydrolase (GH) of the human pathogen . X-ray analysis identifies it as a protein homodimer. The two active sites of the homodimer comprise catalytic residues provided by each monomer. This arrangement is seen in <2% of the hydrolases of known structure. substrate profiling shows BglX is a catalyst for β-(1→2) and β-(1→3) saccharide hydrolysis. Saccharides with β-(1→4) or β-(1→6) bonds, and the β-(1→4) muropeptides from the cell-wall peptidoglycan, are not substrates. Additional structural insights from X-ray analysis (including structures of a mutant enzyme-derived Michaelis complex, two transition-state mimetics, and two enzyme-product complexes) enabled the comprehensive description of BglX catalysis. The half-chair () conformation of the transition-state oxocarbenium species, the approach of the hydrolytic water molecule to the oxocarbenium species, and the stepwise release of the two reaction products were also visualized. The substrate pattern for BglX aligns with the [β-(1→2)-Glc] and [β-(1→3)-Glc] periplasmic osmoregulated periplasmic glucans, and possibly with the Psl exopolysaccharides, of . Both polysaccharides are implicated in biofilm formation. Accordingly, we show that inactivation of the gene of PAO1 attenuates biofilm formation.

PubMed: 31877028
DOI: 10.1021/acschembio.9b00754

実験手法

X-RAY DIFFRACTION (1.8 Å)