2v4a: Difference between revisions
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[[Image:2v4a.gif|left|200px]] | [[Image:2v4a.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE SEMET-LABELED PROLYL-4 HYDROXYLASE (P4H) TYPE I FROM GREEN ALGAE CHLAMYDOMONAS REINHARDTII.''' | {{Structure | ||
|PDB= 2v4a |SIZE=350|CAPTION= <scene name='initialview01'>2v4a</scene>, resolution 1.93Å | |||
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Cl+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:Cl+Binding+Site+For+Chain+D'>AC4</scene>, <scene name='pdbsite=AC5:Gol+Binding+Site+For+Chain+C'>AC5</scene>, <scene name='pdbsite=AC6:Gol+Binding+Site+For+Chain+B'>AC6</scene>, <scene name='pdbsite=AC7:Gol+Binding+Site+For+Chain+A'>AC7</scene>, <scene name='pdbsite=AC8:Gol+Binding+Site+For+Chain+D'>AC8</scene>, <scene name='pdbsite=AC9:Dms+Binding+Site+For+Chain+B'>AC9</scene>, <scene name='pdbsite=BC1:Dms+Binding+Site+For+Chain+B'>BC1</scene> and <scene name='pdbsite=BC2:So4+Binding+Site+For+Chain+A'>BC2</scene> | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE SEMET-LABELED PROLYL-4 HYDROXYLASE (P4H) TYPE I FROM GREEN ALGAE CHLAMYDOMONAS REINHARDTII.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2V4A is a [ | 2V4A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V4A OCA]. | ||
==Reference== | ==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:// | 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://www.ncbi.nlm.nih.gov/pubmed/17940281 17940281] | ||
[[Category: Chlamydomonas reinhardtii]] | [[Category: Chlamydomonas reinhardtii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:43:09 2008'' | ||
Revision as of 19:43, 20 March 2008
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| , resolution 1.93Å | |||||||
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| Sites: | , , , , , , , , , and | ||||||
| Ligands: | , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE SEMET-LABELED PROLYL-4 HYDROXYLASE (P4H) TYPE I FROM GREEN ALGAE CHLAMYDOMONAS REINHARDTII.
OverviewOverview
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.
About this StructureAbout this Structure
2V4A is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.
ReferenceReference
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
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