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<ref>pmid 19553701</ref>. | 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<ref>pmid 19553701</ref>. | ||
| - | == Function == | + | == Function == |
Prolyl 4-hydroxylase (P4H) catalyses the hydroxylation of a proline resiue in the collagens . | Prolyl 4-hydroxylase (P4H) catalyses the hydroxylation of a proline resiue in the collagens . | ||
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== Relevance == | == Relevance == | ||
P4H belongs to the super family of 2-oxoglutarate dioxygenases. | P4H belongs to the super family of 2-oxoglutarate dioxygenases. | ||
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== Structural highlights == | == Structural highlights == | ||
| + | All the green links below show [[morphs]] created with the [http://proteopedia.org/cgi-bin/morph Proteopedia/PyMOL Morpher]. | ||
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Two <scene name='80/809814/Zncomplex-to-sp5structure/1'>flexible loops</scene> are important for the peptide binding. | Two <scene name='80/809814/Zncomplex-to-sp5structure/1'>flexible loops</scene> are important for the peptide binding. | ||
Current revision
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References
- ↑ 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
