2v4a
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CRYSTAL STRUCTURE OF THE SEMET-LABELED PROLYL-4 HYDROXYLASE (P4H) TYPE I FROM GREEN ALGAE CHLAMYDOMONAS REINHARDTII.
OverviewOverview
Prolyl 4-hydroxylases (P4Hs) are 2-oxoglutarate dioxygenases that catalyze, the hydroxylation of peptidyl prolines. They play an important role in, collagen synthesis, oxygen homeostasis, and plant cell wall formation. We, describe four structures of a P4H from the green alga Chlamydomonas, reinhardtii, two of the apoenzyme at 1.93 and 2.90A resolution, one, complexed with the competitive inhibitor Zn(2+), and one with Zn(2+) and, pyridine 2,4-dicarboxylate (which is an analogue of 2-oxoglutarate) at, 1.85A resolution. The structures reveal the double-stranded beta-helix, core fold (jellyroll motif), typical for 2-oxoglutarate dioxygenases. The, catalytic site is at the center of an extended shallow groove lined by two, flexible loops. Mutagenesis studies together with the crystallographic, data indicate that this groove participates in the binding of the, proline-rich peptide-substrates. It is discussed that the algal P4H and, the catalytic domain of collagen P4Hs have notable structural, similarities, suggesting that these enzymes form a separate structural, subgroup of P4Hs different from the hypoxia-inducible factor P4Hs. Key, structural differences between these two subgroups are described. These, studies provide first insight into the structure-function relationships of, the collagen P4Hs, which unlike the hypoxia-inducible factor P4Hs use, proline-rich peptides as their substrates.
About this StructureAbout this Structure
2V4A is a Single protein structure of sequence from Chlamydomonas reinhardtii with , , and as ligands. Known structural/functional Sites: , , , , , , , , , and . Full crystallographic information is available from OCA.
ReferenceReference
The active site of an algal prolyl 4-hydroxylase has a large structural plasticity., Koski MK, Hieta R, Bollner C, Kivirikko KI, Myllyharju J, Wierenga RK, J Biol Chem. 2007 Dec 21;282(51):37112-23. Epub 2007 Oct 16. PMID:17940281
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