1c25: Difference between revisions
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==Overview== | ==Overview== | ||
Cdc25 phosphatases activate the cell division kinases throughout the cell, cycle. The 2.3 A structure of the human Cdc25A catalytic domain reveals a, small alpha/beta domain with a fold unlike previously described, phosphatase structures but identical to rhodanese, a sulfur-transfer, protein. Only the active-site loop, containing the Cys-(X)5-Arg motif, shows similarity to the tyrosine phosphatases. In some crystals, the, catalytic Cys-430 forms a disulfide bond with the invariant Cys-384, suggesting that Cdc25 may be self-inhibited during oxidative stress., Asp-383, previously proposed to be the general acid, instead serves a, structural role, forming a conserved buried salt-bridge. We propose that, Glu-431 may act as a general acid. Structure-based alignments suggest that, the . | Cdc25 phosphatases activate the cell division kinases throughout the cell, cycle. The 2.3 A structure of the human Cdc25A catalytic domain reveals a, small alpha/beta domain with a fold unlike previously described, phosphatase structures but identical to rhodanese, a sulfur-transfer, protein. Only the active-site loop, containing the Cys-(X)5-Arg motif, shows similarity to the tyrosine phosphatases. In some crystals, the, catalytic Cys-430 forms a disulfide bond with the invariant Cys-384, suggesting that Cdc25 may be self-inhibited during oxidative stress., Asp-383, previously proposed to be the general acid, instead serves a, structural role, forming a conserved buried salt-bridge. We propose that, Glu-431 may act as a general acid. Structure-based alignments suggest that, the noncatalytic domain of the MAP kinase phosphatases will share this, topology, as will ACR2, a eukaryotic arsenical resistance protein. | ||
==About this Structure== | ==About this Structure== | ||
1C25 is a | 1C25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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] Structure known Active Sites: DSU and POP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C25 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:47:08 2007'' | ||
