7TPU

Crystal structure of a chitinase-modifying protein from Fusarium vanettenii (Fvan-cmp)

7TPU の概要

• エントリーDOI: 10.2210/pdb7tpu/pdb
• 分子名称: Beta-lactamase domain-containing protein, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: polyglycine hydrolase, chitinase-modifying protein, serine protease, beta lactamase-like, hydrolase
• 由来する生物種: Fusarium vanettenii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 69586.82

構造登録者

Dowling, N.V.,Naumann, T.A.,Price, N.P.J.,Rose, D.R. (登録日: 2022-01-26, 公開日: 2023-02-15, 最終更新日: 2024-11-06)

主引用文献

Dowling, N.V.,Naumann, T.A.,Price, N.P.J.,Rose, D.R.
Crystal structure of a polyglycine hydrolase determined using a RoseTTAFold model.
Acta Crystallogr D Struct Biol, 79:168-176, 2023

PubMed Abstract: Polyglycine hydrolases (PGHs) are secreted fungal proteases that cleave the polyglycine linker of Zea mays ChitA, a defensive chitinase, thus overcoming one mechanism of plant resistance to infection. Despite their importance in agriculture, there has been no previous structural characterization of this family of proteases. The objective of this research was to investigate the proteolytic mechanism and other characteristics by structural and biochemical means. Here, the first atomic structure of a polyglycine hydrolase was identified. It was solved by X-ray crystallography using a RoseTTAFold model, taking advantage of recent technical advances in structure prediction. PGHs are composed of two domains: the N- and C-domains. The N-domain is a novel tertiary fold with an as-yet unknown function that is found across all kingdoms of life. The C-domain shares structural similarities with class C β-lactamases, including a common catalytic nucleophilic serine. In addition to insights into the PGH family and its relationship to β-lactamases, the results demonstrate the power of complementing experimental structure determination with new computational techniques.

PubMed: 36762862
DOI: 10.1107/S2059798323000311

実験手法

X-RAY DIFFRACTION (2.194 Å)