3S5O

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

Summary for 3S5O

• Entry DOI: 10.2210/pdb3s5o/pdb
• Related: 3S5N
• Descriptor: 4-hydroxy-2-oxoglutarate aldolase, mitochondrial, 1,2-ETHANEDIOL, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: aldolase, beta barrel, schiff base, hydroxyproline metabolism, lyase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion (By similarity): Q86XE5
• Total number of polymer chains: 1
• Total formula weight: 33391.28

Authors

Riedel, T.J.,Lowther, W.T. (deposition date: 2011-05-23, release date: 2011-10-26)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.97 Å)