User:Kristian Koski/P4H

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-==Your Heading Here (maybe something like 'Structure')==
+<StructureSection load='3gze' size='340' side='right' caption='Caption for this structure' scene=''>
-<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
+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>.
-This is a default text for your page '''Kristian Koski/P4H'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
-You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 == 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 ==
+All the green links below show [[morphs]] created with the [http://proteopedia.org/cgi-bin/morph Proteopedia/PyMOL Morpher].
+Two <scene name='80/809814/Zncomplex-to-sp5structure/1'>flexible loops</scene> are important for the peptide binding.
 This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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Caption for this structure

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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].

1 Function
2 Disease
3 Relevance
4 Structural highlights

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

All the green links below show morphs created with the Proteopedia/PyMOL Morpher.

Two are important for the peptide binding.

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

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