6YGE

NADase from Aspergillus fumigatus

6YGE の概要

• エントリーDOI: 10.2210/pdb6yge/pdb
• 分子名称: AfNADase, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: nad+ glycohydrolase, nad, ca-binding, homodimer, glycoprotein, hydrolase
• 由来する生物種: Aspergillus fumigatus Af293
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58013.71

構造登録者

Stromland, O.,Ziegler, M.,Kallio, J.P. (登録日: 2020-03-27, 公開日: 2020-12-23, 最終更新日: 2024-11-13)

主引用文献

Stromland, O.,Kallio, J.P.,Pschibul, A.,Skoge, R.H.,Hardardottir, H.M.,Sverkeli, L.J.,Heinekamp, T.,Kniemeyer, O.,Migaud, M.,Makarov, M.V.,Gossmann, T.I.,Brakhage, A.A.,Ziegler, M.
Discovery of fungal surface NADases predominantly present in pathogenic species.
Nat Commun, 12:1631-1631, 2021

PubMed Abstract: Nicotinamide adenine dinucleotide (NAD) is a key molecule in cellular bioenergetics and signalling. Various bacterial pathogens release NADase enzymes into the host cell that deplete the host's NAD pool, thereby causing rapid cell death. Here, we report the identification of NADases on the surface of fungi such as the pathogen Aspergillus fumigatus and the saprophyte Neurospora crassa. The enzymes harbour a tuberculosis necrotizing toxin (TNT) domain and are predominately present in pathogenic species. The 1.6 Å X-ray structure of the homodimeric A. fumigatus protein reveals unique properties including N-linked glycosylation and a Ca-binding site whose occupancy regulates activity. The structure in complex with a substrate analogue suggests a catalytic mechanism that is distinct from those of known NADases, ADP-ribosyl cyclases and transferases. We propose that fungal NADases may convey advantages during interaction with the host or competing microorganisms.

PubMed: 33712585
DOI: 10.1038/s41467-021-21307-z

実験手法

X-RAY DIFFRACTION (1.6 Å)