7E6J

Aspartyl/Asparaginyl beta-hydroxylase (AspH) H725A in complex with Factor X peptide fragment (39mer-4Ser)

7E6J の概要

• エントリーDOI: 10.2210/pdb7e6j/pdb
• 分子名称: Aspartyl/asparaginyl beta-hydroxylase, Peptide from Factor X light chain, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: aspartyl/asparaginyl beta-hydroxylase, dioxygenase, oxidoreductase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53879.01

構造登録者

Nakashima, Y.,Brasnett, A.,Brewitz, L.,Schofield, C.J. (登録日: 2021-02-22, 公開日: 2021-06-30, 最終更新日: 2024-11-20)

主引用文献

Brasnett, A.,Pfeffer, I.,Brewitz, L.,Chowdhury, R.,Nakashima, Y.,Tumber, A.,McDonough, M.A.,Schofield, C.J.
Human Oxygenase Variants Employing a Single Protein Fe II Ligand Are Catalytically Active.
Angew.Chem.Int.Ed.Engl., 60:14657-14663, 2021

PubMed Abstract: Aspartate/asparagine-β-hydroxylase (AspH) is a human 2-oxoglutarate (2OG) and Fe oxygenase that catalyses C3 hydroxylations of aspartate/asparagine residues of epidermal growth factor-like domains (EGFDs). Unusually, AspH employs two histidine residues to chelate Fe rather than the typical triad of two histidine and one glutamate/aspartate residue. We report kinetic, inhibition, and crystallographic studies concerning human AspH variants in which either of its Fe binding histidine residues are substituted for alanine. Both the H725A and, in particular, the H679A AspH variants retain substantial catalytic activity. Crystal structures clearly reveal metal-ligation by only a single protein histidine ligand. The results have implications for the functional assignment of 2OG oxygenases and for the design of non-protein biomimetic catalysts.

PubMed: 33887099
DOI: 10.1002/anie.202103711

実験手法

X-RAY DIFFRACTION (1.9 Å)