1ym9: Difference between revisions
New page: left|200px<br /> <applet load="1ym9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ym9, resolution 2.00Å" /> '''Crystal structure o... |
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caption="1ym9, resolution 2.00Å" /> | caption="1ym9, resolution 2.00Å" /> | ||
'''Crystal structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the sulfinic form'''<br /> | '''Crystal structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the sulfinic form'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1YM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1YM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YM9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: sulfinic cysteine]] | [[Category: sulfinic cysteine]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:12:12 2008'' | ||
Revision as of 18:12, 15 February 2008
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Crystal structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the sulfinic form
OverviewOverview
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 StructureAbout this Structure
1YM9 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
ReferenceReference
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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