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Literature summary for 1.14.11.29 extracted from

  • Myllykoski, M.; Sutinen, A.; Koski, M.; Kallio, J.; Raasakka, A.; Myllyharju, J.; Wierenga, R.; Koivunen, P.
    Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains (2021), J. Biol. Chem., 296, 100197 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor-diffusion method, the crystal structure reveals an EF domain with two Ca2+-binding motifs inserted within the catalytic domain. A substrate-binding groove is formed between the EF domain and the conserved core of the catalytic domain Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum the enzyme is composed of an N-terminal cytoplasmic tail, a membrane-anchoring transmembrane helix, and a unique combination of a Ca2+-binding EF domain and a catalytic domain that is located within the ER lumen membrane Homo sapiens 5783
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Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the crystal structure reveals an EF domain with two Ca2+-binding motifs inserted within the catalytic domain. The proximity of the EF domain to the active site suggests that Ca2+ binding is relevant to the catalytic activity. Functional analysis demonstrates that Ca2+-binding affinity of P4H-TM is within the range of physiological Ca2+ concentration in the endoplasmic reticulum. P4H-TM is found both as a monomer and a dimer in the solution, but the monomer-dimer equilibrium is not regulated by Ca2+ Homo sapiens
Fe2+ the catalytic site contained bound Fe2+ and N-oxalylglycine Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9NXG6
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Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
P4H-TM
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 Homo sapiens
transmembrane prolyl 4-hydroxylase
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 Homo sapiens

General Information

General Information Comment Organism
physiological function prolyl 4-hydroxylases (P4Hs) catalyze post-translational hydroxylation of peptidyl proline residues Homo sapiens