7U3A

Structure of the Streptomyces venezuelae GlgX-c-di-GMP complex

7U3A の概要

• エントリーDOI: 10.2210/pdb7u3a/pdb
• 分子名称: Glycogen debranching enzyme GlgX, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) (2 entities in total)
• 機能のキーワード: c-di-gmp, glgx, glycogen, glycogen debranching enzyme, second messenger, development, streptomyces, hydrolase
• 由来する生物種: Streptomyces venezuelae
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 323430.58

構造登録者

Schumacher, M.A. (登録日: 2022-02-26, 公開日: 2022-10-05, 最終更新日: 2023-10-18)

主引用文献

Schumacher, M.A.,Wormann, M.E.,Henderson, M.,Salinas, R.,Latoscha, A.,Al-Bassam, M.M.,Singh, K.S.,Barclay, E.,Gunka, K.,Tschowri, N.
Allosteric regulation of glycogen breakdown by the second messenger cyclic di-GMP.
Nat Commun, 13:5834-5834, 2022

PubMed Abstract: Streptomyces are our principal source of antibiotics, which they generate concomitant with a complex developmental transition from vegetative hyphae to spores. c-di-GMP acts as a linchpin in this transition by binding and regulating the key developmental regulators, BldD and WhiG. Here we show that c-di-GMP also binds the glycogen-debranching-enzyme, GlgX, uncovering a direct link between c-di-GMP and glycogen metabolism in bacteria. Further, we show c-di-GMP binding is required for GlgX activity. We describe structures of apo and c-di-GMP-bound GlgX and, strikingly, their comparison shows c-di-GMP induces long-range conformational changes, reorganizing the catalytic pocket to an active state. Glycogen is an important glucose storage compound that enables animals to cope with starvation and stress. Our in vivo studies reveal the important biological role of GlgX in Streptomyces glucose availability control. Overall, we identify a function of c-di-GMP in controlling energy storage metabolism in bacteria, which is widespread in Actinobacteria.

PubMed: 36192422
DOI: 10.1038/s41467-022-33537-w

実験手法

X-RAY DIFFRACTION (3.34 Å)