7B3N

AmiP amidase-3 from Thermus parvatiensis

7B3N の概要

• エントリーDOI: 10.2210/pdb7b3n/pdb
• 分子名称: Cell wall hydrolase, ZINC ION, GLYCEROL, ... (8 entities in total)
• 機能のキーワード: amidase-3 thermophilic, hydrolase
• 由来する生物種: Thermus parvatiensis
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 98555.09

構造登録者

Freitag-Pohl, S.,Pohl, E. (登録日: 2020-12-01, 公開日: 2022-06-22, 最終更新日: 2024-06-19)

主引用文献

Jasilionis, A.,Plotka, M.,Wang, L.,Dorawa, S.,Lange, J.,Watzlawick, H.,van den Bergh, T.,Vroling, B.,Altenbuchner, J.,Kaczorowska, A.K.,Pohl, E.,Kaczorowski, T.,Nordberg Karlsson, E.,Freitag-Pohl, S.
AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase.
Protein Sci., 32:e4585-e4585, 2023

PubMed Abstract: Bacteriophages encode a wide variety of cell wall disrupting enzymes that aid the viral escape in the final stages of infection. These lytic enzymes have accumulated notable interest due to their potential as novel antibacterials for infection treatment caused by multiple-drug resistant bacteria. Here, the detailed functional and structural characterization of Thermus parvatiensis prophage peptidoglycan lytic amidase AmiP, a globular Amidase_3 type lytic enzyme adapted to high temperatures is presented. The sequence and structure comparison with homologous lytic amidases reveals the key adaptation traits that ensure the activity and stability of AmiP at high temperatures. The crystal structure determined at a resolution of 1.8 Å displays a compact α/β-fold with multiple secondary structure elements omitted or shortened compared with protein structures of similar proteins. The functional characterization of AmiP demonstrates high efficiency of catalytic activity and broad substrate specificity toward thermophilic and mesophilic bacteria strains containing Orn-type or DAP-type peptidoglycan. The here presented AmiP constitutes the most thermoactive and ultrathermostable Amidase_3 type lytic enzyme biochemically characterized with a temperature optimum at 85°C. The extraordinary high melting temperature T 102.6°C confirms fold stability up to approximately 100°C. Furthermore, AmiP is shown to be more active over the alkaline pH range with pH optimum at pH 8.5 and tolerates NaCl up to 300 mM with the activity optimum at 25 mM NaCl. This set of beneficial characteristics suggests that AmiP can be further exploited in biotechnology.

PubMed: 36721347
DOI: 10.1002/pro.4585

実験手法

X-RAY DIFFRACTION (1.793 Å)