6C62

An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme.

6C62 の概要

• エントリーDOI: 10.2210/pdb6c62/pdb
• 分子名称: Biuret hydrolase, AtzG, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: atze; biuret hydrolase; atrazine; cyanuric acid; ser-cisser-lys hydrolase, hydrolase
• 由来する生物種: Pseudomonas sp. (strain ADP); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 111299.57

構造登録者

Peat, T.S.,Esquirol, L.,Wilding, M.,Liu, J.W.,French, N.G.,Hartley, C.J.,Hideki, O.,Easton, C.J.,Newman, J.,Scott, C. (登録日: 2018-01-17, 公開日: 2018-03-21, 最終更新日: 2023-11-15)

主引用文献

Esquirol, L.,Peat, T.S.,Wilding, M.,Liu, J.W.,French, N.G.,Hartley, C.J.,Onagi, H.,Nebl, T.,Easton, C.J.,Newman, J.,Scott, C.
An unexpected vestigial protein complex reveals the evolutionary origins of ans-triazine catabolic enzyme.
J. Biol. Chem., 293:7880-7891, 2018

PubMed Abstract: Cyanuric acid is a metabolic intermediate of -triazines, such as atrazine (a common herbicide) and melamine (used in resins and plastics). Cyanuric acid is mineralized to ammonia and carbon dioxide by the soil bacterium sp. strain ADP via three hydrolytic enzymes (AtzD, AtzE, and AtzF). Here, we report the purification and biochemical and structural characterization of AtzE. Contrary to previous reports, we found that AtzE is not a biuret amidohydrolase, but instead it catalyzes the hydrolytic deamination of 1-carboxybiuret. X-ray crystal structures of apo AtzE and AtzE bound with the suicide inhibitor phenyl phosphorodiamidate revealed that the AtzE enzyme complex consists of two independent molecules in the asymmetric unit. We also show that AtzE forms an α2β2 heterotetramer with a previously unidentified 68-amino acid-long protein (AtzG) encoded in the cyanuric acid mineralization operon from sp. strain ADP. Moreover, we observed that AtzG is essential for the production of soluble, active AtzE and that this obligate interaction is a vestige of their shared evolutionary origin. We propose that AtzEG was likely recruited into the cyanuric acid-mineralizing pathway from an ancestral glutamine transamidosome that required protein-protein interactions to enforce the exclusion of solvent from the transamidation reaction.

PubMed: 29523689
DOI: 10.1074/jbc.RA118.001996

実験手法

X-RAY DIFFRACTION (1.95 Å)