User:Kristian Koski/P4H

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Chlamydomonas reinhardtii prolyl 4-hydroxylase is a monomeric enzyme which catalyse the hydroxylation of proline residues of the proline-rich cell wall proteins. The structure of Cr-P4H has been determined as apo and in complexed with Zinc and serine-proline rich peptide[1].

Contents

Function

Prolyl 4-hydroxylase (P4H) catalyses the hydroxylation of a proline resiue in the collagens .

Disease

Relevance

P4H belongs to the super family of 2-oxoglutarate dioxygenases.

Structural highlights

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Two flexible loops are important for the peptide binding.

This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


Caption for this structure

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References

  1. ↑ Koski MK, Hieta R, Hirsila M, Ronka A, Myllyharju J, Wierenga RK. The crystal structure of an algal prolyl 4-hydroxylase complexed with a proline-rich peptide reveals a novel buried tripeptide binding motif. J Biol Chem. 2009 Sep 11;284(37):25290-301. Epub 2009 Jun 24. PMID:19553701 doi:10.1074/jbc.M109.014050

Proteopedia Page Contributors and Editors (what is this?)

Kristian Koski, Eric Martz

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