7PU1

High resolution X-ray structure of Thermoascus aurantiacus LPMO

これはPDB形式変換不可エントリーです。

7PU1 の概要

• エントリーDOI: 10.2210/pdb7pu1/pdb
• 関連するPDBエントリー: 7PTZ
• 分子名称: Gh61 isozyme a, COPPER (II) ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: copper binding protein, beta-sandwich fold, auxillary, oxidoreductase
• 由来する生物種: Thermoascus aurantiacus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50079.20

構造登録者

Banerjee, S.,Frandsen, K.E.H.,Singh, R.K.,Bjerrum, M.J.,Lo Leggio, L. (登録日: 2021-09-28, 公開日: 2022-03-16, 最終更新日: 2024-01-31)

主引用文献

Banerjee, S.,Muderspach, S.J.,Tandrup, T.,Frandsen, K.E.H.,Singh, R.K.,Ipsen, J.O.,Hernandez-Rollan, C.,Norholm, M.H.H.,Bjerrum, M.J.,Johansen, K.S.,Lo Leggio, L.
Protonation State of an Important Histidine from High Resolution Structures of Lytic Polysaccharide Monooxygenases.
Biomolecules, 12:-, 2022

PubMed Abstract: Lytic Polysaccharide Monooxygenases (LPMOs) oxidatively cleave recalcitrant polysaccharides. The mechanism involves (i) reduction of the Cu, (ii) polysaccharide binding, (iii) binding of different oxygen species, and (iv) glycosidic bond cleavage. However, the complete mechanism is poorly understood and may vary across different families and even within the same family. Here, we have investigated the protonation state of a secondary co-ordination sphere histidine, conserved across AA9 family LPMOs that has previously been proposed to be a potential proton donor. Partial unrestrained refinement of newly obtained higher resolution data for two AA9 LPMOs and re-refinement of four additional data sets deposited in the PDB were carried out, where the His was refined without restraints, followed by measurements of the His ring geometrical parameters. This allowed reliable assignment of the protonation state, as also validated by following the same procedure for the His brace, for which the protonation state is predictable. The study shows that this histidine is generally singly protonated at the Nε2 atom, which is close to the oxygen species binding site. Our results indicate robustness of the method. In view of this and other emerging evidence, a role as proton donor during catalysis is unlikely for this His.

PubMed: 35204695
DOI: 10.3390/biom12020194

実験手法

X-RAY DIFFRACTION (1.06 Å)