7P9B

Providencia stuartii Arginine decarboxylase (Adc), decamer structure

7P9B の概要

• エントリーDOI: 10.2210/pdb7p9b/pdb
• EMDBエントリー: 13261
• 分子名称: Biodegradative arginine decarboxylase (1 entity in total)
• 機能のキーワード: decarboxylase, laodc, plp-dependant enzyme, adc, lyase
• 由来する生物種: Providencia stuartii
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 861502.50

構造登録者

Jessop, M.,Desfosses, A.,Bacia-Verloop, M.,Gutsche, I. (登録日: 2021-07-26, 公開日: 2022-04-20)

主引用文献

Jessop, M.,Huard, K.,Desfosses, A.,Tetreau, G.,Carriel, D.,Bacia-Verloop, M.,Mas, C.,Mas, P.,Fraudeau, A.,Colletier, J.P.,Gutsche, I.
Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation.
Commun Biol, 5:317-317, 2022

PubMed Abstract: Bacterial homologous lysine and arginine decarboxylases play major roles in the acid stress response, physiology, antibiotic resistance and virulence. The Escherichia coli enzymes are considered as their archetypes. Whereas acid stress triggers polymerisation of the E. coli lysine decarboxylase LdcI, such behaviour has not been observed for the arginine decarboxylase Adc. Here we show that the Adc from a multidrug-resistant human pathogen Providencia stuartii massively polymerises into filaments whose cryo-EM structure reveals pronounced differences between Adc and LdcI assembly mechanisms. While the structural determinants of Adc polymerisation are conserved only in certain Providencia and Burkholderia species, acid stress-induced polymerisation of LdcI appears general for enterobacteria. Analysis of the expression, activity and oligomerisation of the P. stuartii Adc further highlights the distinct properties of this unusual protein and lays a platform for future investigation of the role of supramolecular assembly in the superfamily or arginine and lysine decarboxylases.

PubMed: 35383285
DOI: 10.1038/s42003-022-03276-1

実験手法

ELECTRON MICROSCOPY (2.45 Å)