1ymk
From Proteopedia
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| - | [[Image:1ymk.jpg|left|200px]] | + | [[Image:1ymk.jpg|left|200px]] |
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| - | '''Crystal Structure of the CDC25B phosphatase catalytic domain in the apo form''' | + | {{Structure |
| + | |PDB= 1ymk |SIZE=350|CAPTION= <scene name='initialview01'>1ymk</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] | ||
| + | |GENE= CDC25B, CDC25HU2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of the CDC25B phosphatase catalytic domain in the apo form''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YMK is a [ | + | 1YMK 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=1YMK OCA]. |
==Reference== | ==Reference== | ||
| - | Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond., Buhrman G, Parker B, Sohn J, Rudolph J, Mattos C, Biochemistry. 2005 Apr 12;44(14):5307-16. PMID:[http:// | + | Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond., Buhrman G, Parker B, Sohn J, Rudolph J, Mattos C, Biochemistry. 2005 Apr 12;44(14):5307-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15807524 15807524] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
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[[Category: apo enzyme]] | [[Category: apo enzyme]] | ||
| - | ''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 15:24:52 2008'' |
Revision as of 13:24, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | |||||||
| Gene: | CDC25B, CDC25HU2 (Homo sapiens) | ||||||
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the CDC25B phosphatase catalytic domain in the apo form
Overview
Cdc25B phosphatase, an important regulator of the cell cycle, forms an intramolecular disulfide bond in response to oxidation leading to reversible inactivation of phosphatase activity. We have obtained a crystallographic time course revealing the structural rearrangements that occur in the P-loop as the enzyme goes from its apo state, through the sulfenic (Cys-SO(-)) intermediate, to the stable disulfide. We have also obtained the structures of the irreversibly oxidized sulfinic (Cys-SO(2)(-)) and sulfonic (Cys-SO(3)(-)) Cdc25B. The active site P-loop is found in three conformations. In the apoenzyme, the P-loop is in the active conformation. In the sulfenic intermediate, the P-loop partially obstructs the active site cysteine, poised to undergo the conformational changes that accompany disulfide bond formation. In the disulfide form, the P-loop is closed over the active site cysteine, resulting in an enzyme that is unable to bind substrate. The structural changes that occur in the sulfenic intermediate of Cdc25B are distinctly different from those seen in protein tyrosine phosphatase 1B where a five-membered sulfenyl amide ring is generated as the stable end product. This work elucidates the mechanism by which chemistry and structure are coupled in the regulation of Cdc25B by reactive oxygen species.
About this Structure
1YMK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond., Buhrman G, Parker B, Sohn J, Rudolph J, Mattos C, Biochemistry. 2005 Apr 12;44(14):5307-16. PMID:15807524
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