6TKU

Crystal structure of a capsule-specific depolymerase produced by Klebsiella phage

6TKU の概要

• エントリーDOI: 10.2210/pdb6tku/pdb
• 分子名称: depolymerase KP32gp38 (2 entities in total)
• 機能のキーワード: klebsiella pneumoniae capsule, phage depolymerase, tail fiber branching system, hydrolase
• 由来する生物種: Klebsiella phage KP32
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 63317.25

構造登録者

Berisio, R.,Squeglia, F. (登録日: 2019-11-29, 公開日: 2020-04-22, 最終更新日: 2024-10-16)

主引用文献

Squeglia, F.,Maciejewska, B.,Latka, A.,Ruggiero, A.,Briers, Y.,Drulis-Kawa, Z.,Berisio, R.
Structural and Functional Studies of a Klebsiella Phage Capsule Depolymerase Tailspike: Mechanistic Insights into Capsular Degradation.
Structure, 28:613-, 2020

PubMed Abstract: Capsule polysaccharide is a major virulence factor of Klebsiella pneumoniae, a nosocomial pathogen associated with a wide range of infections. It protects bacteria from harsh environmental conditions, immune system response, and phage infection. To access cell wall-located receptors, some phages possess tailspike depolymerases that degrade the capsular polysaccharide. Here, we present the crystal structure of a tailspike against Klebsiella, KP32gp38, whose primary sequence shares no similarity to other proteins of known structure. In the trimeric structure of KP32gp38, each chain contains a flexible N-terminal domain, a right-handed parallel β helix domain and two β sandwiches with carbohydrate binding features. The crystal structure and activity assays allowed us to locate the catalytic site. Also, our data provide experimental evidence of a branching architecture of depolymerases in KP32 Klebsiella viruses, as KP32gp38 displays nanomolar affinity to another depolymerase from the same phage, KP32gp37. Results provide a structural framework for enzyme engineering to produce serotype-broad-active enzyme complexes against K. pneumoniae.

PubMed: 32386574
DOI: 10.1016/j.str.2020.04.015

実験手法

X-RAY DIFFRACTION (1.8 Å)