2obi
From Proteopedia
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| - | [[Image:2obi.jpg|left|200px]] | + | [[Image:2obi.jpg|left|200px]] |
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| - | '''Crystal structure of the Selenocysteine to Cysteine Mutant of human phospholipid hydroperoxide glutathione peroxidase (GPx4)''' | + | {{Structure |
| + | |PDB= 2obi |SIZE=350|CAPTION= <scene name='initialview01'>2obi</scene>, resolution 1.55Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipid-hydroperoxide_glutathione_peroxidase Phospholipid-hydroperoxide glutathione peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.12 1.11.1.12] | ||
| + | |GENE= GPX4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the Selenocysteine to Cysteine Mutant of human phospholipid hydroperoxide glutathione peroxidase (GPx4)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OBI is a [ | + | 2OBI 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=2OBI OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4)., Scheerer P, Borchert A, Krauss N, Wessner H, Gerth C, Hohne W, Kuhn H, Biochemistry. 2007 Aug 7;46(31):9041-9. Epub 2007 Jul 13. PMID:[http:// | + | Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4)., Scheerer P, Borchert A, Krauss N, Wessner H, Gerth C, Hohne W, Kuhn H, Biochemistry. 2007 Aug 7;46(31):9041-9. Epub 2007 Jul 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17630701 17630701] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Phospholipid-hydroperoxide glutathione peroxidase]] | [[Category: Phospholipid-hydroperoxide glutathione peroxidase]] | ||
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[[Category: thioredoxin-fold]] | [[Category: thioredoxin-fold]] | ||
| - | ''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 17:57:33 2008'' |
Revision as of 15:57, 20 March 2008
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| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | GPX4 (Homo sapiens) | ||||||
| Activity: | Phospholipid-hydroperoxide glutathione peroxidase, with EC number 1.11.1.12 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Selenocysteine to Cysteine Mutant of human phospholipid hydroperoxide glutathione peroxidase (GPx4)
Overview
Phospholipid hydroperoxide glutathione peroxidase (GPx4) is a moonlighting selenoprotein, which has been implicated in anti-oxidative defense, sperm development, and cerebral embryogenesis. Among GPx-isoforms, GPx4 is unique because of its capability to reduce complex lipid hydroperoxides and its tendency toward polymerization, but the structural basis for these properties remained unclear. To address this, we solved the crystal structure of the catalytically active U46C mutant of human GPx4 to 1.55 A resolution. X-ray data indicated a monomeric protein consisting of four alpha-helices and seven beta-strands. GPx4 lacks a surface exposed loop domain, which appears to limit the accessibility of the active site of other GPx-isoforms, and these data may explain the broad substrate specificity of GPx4. The catalytic triad (C46, Q81, and W136) is localized at a flat impression of the protein surface extending into a surface exposed patch of basic amino acids (K48, K135, and R152) that also contains polar T139. Multiple mutations of the catalytic triad indicated its functional importance. Like the wild-type enzyme, the U46C mutant exhibits a strong tendency toward protein polymerization, which was prevented by reductants. Site-directed mutagenesis suggested involvement of the catalytic C46 and surface exposed C10 and C66 in polymer formation. In GPx4 crystals, these residues contact adjacent protein monomers.
About this Structure
2OBI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4)., Scheerer P, Borchert A, Krauss N, Wessner H, Gerth C, Hohne W, Kuhn H, Biochemistry. 2007 Aug 7;46(31):9041-9. Epub 2007 Jul 13. PMID:17630701
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