2jij

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2jij.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2jij.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2jij| PDB=2jij | SCENE= }}
{{STRUCTURE_2jij| PDB=2jij | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE APO FORM OF CHLAMYDOMONAS REINHARDTII PROLYL-4 HYDROXYLASE TYPE I'''
+
===CRYSTAL STRUCTURE OF THE APO FORM OF CHLAMYDOMONAS REINHARDTII PROLYL-4 HYDROXYLASE TYPE I===
-
==Overview==
+
<!--
-
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 2.90 A resolution, one complexed with the competitive inhibitor Zn2+, and one with Zn2+ and pyridine 2,4-dicarboxylate (which is an analogue of 2-oxoglutarate) at 1.85 A 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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17940281}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17940281 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17940281}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Wierenga, R K.]]
[[Category: Wierenga, R K.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:58:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:32:22 2008''

Revision as of 10:32, 27 July 2008

Image:2jij.png

Template:STRUCTURE 2jij

CRYSTAL STRUCTURE OF THE APO FORM OF CHLAMYDOMONAS REINHARDTII PROLYL-4 HYDROXYLASE TYPE I

Template:ABSTRACT PUBMED 17940281

About this Structure

2JIJ is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Sun Jul 27 13:32:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jij"
Personal tools