4CUO

Banyan peroxidase with glycosylation

4CUO の概要

• エントリーDOI: 10.2210/pdb4cuo/pdb
• 分子名称: BANYAN PEROXIDASE, SULFATE ION, CARBONATE ION, ... (12 entities in total)
• 機能のキーワード: oxidoreductase, class iii, glycosylation, succinimide
• 由来する生物種: FICUS BENGHALENSIS (BANYAN TREE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37699.90

構造登録者

Palm, G.J.,Sharma, A.,Hinrichs, W. (登録日: 2014-03-20, 公開日: 2014-07-23, 最終更新日: 2024-11-20)

主引用文献

Palm, G.J.,Sharma, A.,Kumari, M.,Panjikar, S.,Albrecht, D.,Jagannadham, M.V.,Hinrichs, W.
Post-Translational Modification and Extended Glycosylation Pattern of a Plant Latex Peroxidase of Native Source Characterized by X-Ray Crystallography.
FEBS J., 281:4319-, 2014

PubMed Abstract: The crystal structure of banyan peroxidase purified from the latex of Ficus benghalensis has been solved at 1.67 Å resolution by single-wavelength anomalous diffraction phasing. The refined structure includes 306 amino acid residues, a heme and two calcium ions. The protein belongs to class III peroxidases and is the first one from plant latex. Extensive glycosylation was observed with N-linked glycans attached to seven asparagine residues. The enzyme is stable with respect to a wide pH range, temperature, chemical denaturants and organic solvents, probably as a result of its high glycosylation. An unexpected post-translational modification of Asp290 was identified as succinimide moiety. Kinetic parameters of banyan peroxidase have been determined using various hydrogen donor substrates and hydrogen peroxide.

PubMed: 24980207
DOI: 10.1111/FEBS.12900

実験手法

X-RAY DIFFRACTION (1.67 Å)