5MIF

Crystal structure of carboxyl esterase 2 (TmelEST2) from mycorrhizal fungus Tuber melanosporum

5MIF の概要

• エントリーDOI: 10.2210/pdb5mif/pdb
• 分子名称: 'Carboxyl esterase 2, FRAGMENT OF TRITON X-100 (3 entities in total)
• 機能のキーワード: lipase alpha/beta hydrolase fold archaebacterial-like enzymes, hydrolase
• 由来する生物種: Tuber melanosporum Mel28
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 150479.75

構造登録者

Zanotti, G.,Vallese, F.,Cavazzini, D.,Ottonello, S. (登録日: 2016-11-28, 公開日: 2017-08-23, 最終更新日: 2024-05-01)

主引用文献

Cavazzini, D.,Grossi, G.,Levati, E.,Vallese, F.,Montanini, B.,Bolchi, A.,Zanotti, G.,Ottonello, S.
A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mycorrhizal fungus Tuber melanosporum.
Sci Rep, 7:7628-7628, 2017

PubMed Abstract: An increasing number of esterases is being revealed by (meta) genomic sequencing projects, but few of them are functionally/structurally characterized, especially enzymes of fungal origin. Starting from a three-member gene family of secreted putative "lipases/esterases" preferentially expressed in the symbiotic phase of the mycorrhizal fungus Tuber melanosporum ("black truffle"), we show here that these enzymes (TmelEST1-3) are dimeric, heat-resistant carboxylesterases capable of hydrolyzing various short/medium chain p-nitrophenyl esters. TmelEST2 was the most active (kcat = 2302 s for p-nitrophenyl-butyrate) and thermally stable (T = 68.3 °C), while TmelEST3 was the only one displaying some activity on tertiary alcohol esters. X-ray diffraction analysis of TmelEST2 revealed a classical α/β hydrolase-fold structure, with a network of dimer-stabilizing intermolecular interactions typical of archaea esterases. The predicted structures of TmelEST1 and 3 are overall quite similar to that of TmelEST2 but with some important differences. Most notably, the much smaller volume of the substrate-binding pocket and the more acidic electrostatic surface profile of TmelEST1. This was also the only TmelEST capable of hydrolyzing feruloyl-esters, suggestinng a possible role in root cell-wall deconstruction during symbiosis establishment. In addition to their potential biotechnological interest, TmelESTs raise important questions regarding the evolutionary recruitment of archaea-like enzymes into mesophilic subterranean fungi such as truffles.

PubMed: 28794466
DOI: 10.1038/s41598-017-08007-9

実験手法

X-RAY DIFFRACTION (2.141 Å)