2jig
From Proteopedia
(New page: 200px<br /><applet load="2jig" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jig, resolution 1.85Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2jig.gif|left|200px]]<br /><applet load="2jig" size=" | + | [[Image:2jig.gif|left|200px]]<br /><applet load="2jig" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2jig, resolution 1.85Å" /> | caption="2jig, resolution 1.85Å" /> | ||
'''CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII PROLYL-4 HYDROXYLASE TYPE I COMPLEXED WITH ZINC AND PYRIDINE-2,4-DICARBOXYLATE'''<br /> | '''CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII PROLYL-4 HYDROXYLASE TYPE I COMPLEXED WITH ZINC AND PYRIDINE-2,4-DICARBOXYLATE'''<br /> | ||
| + | |||
| + | ==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 2.90A 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 Structure== | ==About this Structure== | ||
| - | 2JIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with ZN, SO4, PD2 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Zn Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:Pd2 Binding Site For Chain A'>AC3</scene>, <scene name='pdbsite=AC4:Zn Binding Site For Chain B'>AC4</scene>, <scene name='pdbsite=AC5:Zn Binding Site For Chain B'>AC5</scene>, <scene name='pdbsite=AC6:Gol Binding Site For Chain A'>AC6</scene> and <scene name='pdbsite=AC7:So4 Binding Site For Chain A'>AC7</scene>. Full crystallographic information is available from [http:// | + | 2JIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=PD2:'>PD2</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Zn Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:Pd2 Binding Site For Chain A'>AC3</scene>, <scene name='pdbsite=AC4:Zn Binding Site For Chain B'>AC4</scene>, <scene name='pdbsite=AC5:Zn Binding Site For Chain B'>AC5</scene>, <scene name='pdbsite=AC6:Gol Binding Site For Chain A'>AC6</scene> and <scene name='pdbsite=AC7:So4 Binding Site For Chain A'>AC7</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JIG 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17940281 17940281] | ||
[[Category: Chlamydomonas reinhardtii]] | [[Category: Chlamydomonas reinhardtii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 19: | Line 25: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:22:34 2008'' |
Revision as of 09:22, 23 January 2008
|
CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII PROLYL-4 HYDROXYLASE TYPE I COMPLEXED WITH ZINC AND PYRIDINE-2,4-DICARBOXYLATE
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 2.90A 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 Structure
2JIG 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.
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 Wed Jan 23 11:22:34 2008
Categories: Chlamydomonas reinhardtii | Single protein | Bollner, C. | Hieta, R. | Kivirikko, K.I. | Koski, K.M. | Myllyharju, J. | Wierenga, R.K. | GOL | PD2 | SO4 | ZN | Hydrolase
