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Article

The crystal structure of an algal prolyl 4-hydroxylase complexed with a proline-rich peptide reveals a novel buried tripeptide binding motif.

The Journal of biological chemistry - 11 Sept 2009

Koski M Kristian, Hieta Reija, Hirsilä Maija, Rönkä Anna, Myllyharju Johanna, Wierenga Rik K

Abstract excerpt

Plant and algal prolyl 4-hydroxylases (P4Hs) are key enzymes in the synthesis of cell wall components. These monomeric enzymes belong to the 2-oxoglutarate dependent superfamily of enzymes characterized by a conserved jelly-roll framework. This algal P4H has high sequence similarity to the catalytic domain of the vertebrate, tetrameric collagen P4Hs, whereas there are distinct sequence differences with the...

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Identifiers

PMID: 19553701
DOI: 10.1074/jbc.M109.014050
PMCID: PMC2757231

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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