3S5O

Crystal Structure of Human 4-hydroxy-2-oxoglutarate Aldolase Bound to Pyruvate

3S5O の概要

• エントリーDOI: 10.2210/pdb3s5o/pdb
• 関連するPDBエントリー: 3S5N
• 分子名称: 4-hydroxy-2-oxoglutarate aldolase, mitochondrial, 1,2-ETHANEDIOL, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: aldolase, beta barrel, schiff base, hydroxyproline metabolism, lyase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion (By similarity): Q86XE5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33391.28

構造登録者

Riedel, T.J.,Lowther, W.T. (登録日: 2011-05-23, 公開日: 2011-10-26, 最終更新日: 2025-03-26)

主引用文献

Riedel, T.J.,Johnson, L.C.,Knight, J.,Hantgan, R.R.,Holmes, R.P.,Lowther, W.T.
Structural and Biochemical Studies of Human 4-hydroxy-2-oxoglutarate Aldolase: Implications for Hydroxyproline Metabolism in Primary Hyperoxaluria.
Plos One, 6:e26021-e26021, 2011

PubMed Abstract: 4-hydroxy-2-oxoglutarate (HOG) aldolase is a unique enzyme in the hydroxyproline degradation pathway catalyzing the cleavage of HOG to pyruvate and glyoxylate. Mutations in this enzyme are believed to be associated with the excessive production of oxalate in primary hyperoxaluria type 3 (PH3), although no experimental data is available to support this hypothesis. Moreover, the identity, oligomeric state, enzymatic activity, and crystal structure of human HOGA have not been experimentally determined.

PubMed: 21998747
DOI: 10.1371/journal.pone.0026021

実験手法

X-RAY DIFFRACTION (1.97 Å)