1iyi
From Proteopedia
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| - | [[Image:1iyi.jpg|left|200px]] | + | [[Image:1iyi.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE''' | + | {{Structure |
| + | |PDB= 1iyi |SIZE=350|CAPTION= <scene name='initialview01'>1iyi</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Prostaglandin-D_synthase Prostaglandin-D synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.99.2 5.3.99.2] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IYI is a [ | + | 1IYI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYI OCA]. |
==Reference== | ==Reference== | ||
| - | Mechanism of metal activation of human hematopoietic prostaglandin D synthase., Inoue T, Irikura D, Okazaki N, Kinugasa S, Matsumura H, Uodome N, Yamamoto M, Kumasaka T, Miyano M, Kai Y, Urade Y, Nat Struct Biol. 2003 Apr;10(4):291-6. PMID:[http:// | + | Mechanism of metal activation of human hematopoietic prostaglandin D synthase., Inoue T, Irikura D, Okazaki N, Kinugasa S, Matsumura H, Uodome N, Yamamoto M, Kumasaka T, Miyano M, Kai Y, Urade Y, Nat Struct Biol. 2003 Apr;10(4):291-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12627223 12627223] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Prostaglandin-D synthase]] | [[Category: Prostaglandin-D synthase]] | ||
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[[Category: hematopoietic prostaglandin d synthase]] | [[Category: hematopoietic prostaglandin d synthase]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
| - | [[Category: | + | [[Category: pgd]] |
[[Category: sigma-class gst]] | [[Category: sigma-class gst]] | ||
| - | ''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 11:56:37 2008'' |
Revision as of 09:56, 20 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Prostaglandin-D synthase, with EC number 5.3.99.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE
Overview
Here we report the crystal structures of human hematopoietic prostaglandin (PG) D synthase bound to glutathione (GSH) and Ca2+ or Mg2+. Using GSH as a cofactor, prostaglandin D synthase catalyzes the isomerization of PGH2 to PGD2, a mediator for allergy response. The enzyme is a homodimer, and Ca2+ or Mg2+ increases its activity to approximately 150% of the basal level, with half maximum effective concentrations of 400 microM for Ca2+ and 50 microM for Mg2+. In the Mg2+-bound form, the ion is octahedrally coordinated by six water molecules at the dimer interface. The water molecules are surrounded by pairs of Asp93, Asp96 and Asp97 from each subunit. Ca(2+) is coordinated by five water molecules and an Asp96 from one subunit. The Asp96 residue in the Ca2+-bound form makes hydrogen bonds with two guanidium nitrogen atoms of Arg14 in the GSH-binding pocket. Mg2+ alters the coordinating water structure and reduces one hydrogen bond between Asp96 and Arg14, thereby changing the interaction between Arg14 and GSH. This effect explains a four-fold reduction in the K(m) of the enzyme for GSH. The structure provides insights into how Ca2+ or Mg2+ binding activates human hematopoietic PGD synthase.
About this Structure
1IYI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Mechanism of metal activation of human hematopoietic prostaglandin D synthase., Inoue T, Irikura D, Okazaki N, Kinugasa S, Matsumura H, Uodome N, Yamamoto M, Kumasaka T, Miyano M, Kai Y, Urade Y, Nat Struct Biol. 2003 Apr;10(4):291-6. PMID:12627223
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