1phr
From Proteopedia
(New page: 200px<br /><applet load="1phr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1phr, resolution 2.1Å" /> '''THE CRYSTAL STRUCTURE...) |
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| - | [[Image:1phr.jpg|left|200px]]<br /><applet load="1phr" size=" | + | [[Image:1phr.jpg|left|200px]]<br /><applet load="1phr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1phr, resolution 2.1Å" /> | caption="1phr, resolution 2.1Å" /> | ||
'''THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE'''<br /> | '''THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein tyrosine phosphorylation and dephosphorylation are central | + | Protein tyrosine phosphorylation and dephosphorylation are central reactions for control of cellular division, differentiation and development. Here we describe the crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase (PTPase), a cytosolic phosphatase present in many mammalian cells. The enzyme catalyses the dephosphorylation of phosphotyrosine-containing substrates, and overexpression of the protein in normal and transformed cells inhibits cell proliferation. The structure of the low-molecular-weight PTPase reveals an alpha/beta protein containing a phosphate-binding loop motif at the amino end of helix alpha 1. This motif includes the essential active-site residues Cys 12 and Arg 18 and bears striking similarities to the active-site motif recently described in the structure of human PTP1B. The structure of the low-molecular-weight PTPase supports a reaction mechanism involving the conserved Cys 12 as an attacking nucleophile in an in-line associative mechanism. The structure also suggests a catalytic role for Asp 129 in the reaction cycle. |
==About this Structure== | ==About this Structure== | ||
| - | 1PHR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 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:// | + | 1PHR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</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=1PHR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ramponi, G.]] | [[Category: Ramponi, G.]] | ||
[[Category: Stefani, M.]] | [[Category: Stefani, M.]] | ||
| - | [[Category: Su, X | + | [[Category: Su, X D.]] |
[[Category: Taddei, N.]] | [[Category: Taddei, N.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: phosphotyrosine protein phosphatase]] | [[Category: phosphotyrosine protein phosphatase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:54 2008'' |
Revision as of 12:28, 21 February 2008
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THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE
Overview
Protein tyrosine phosphorylation and dephosphorylation are central reactions for control of cellular division, differentiation and development. Here we describe the crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase (PTPase), a cytosolic phosphatase present in many mammalian cells. The enzyme catalyses the dephosphorylation of phosphotyrosine-containing substrates, and overexpression of the protein in normal and transformed cells inhibits cell proliferation. The structure of the low-molecular-weight PTPase reveals an alpha/beta protein containing a phosphate-binding loop motif at the amino end of helix alpha 1. This motif includes the essential active-site residues Cys 12 and Arg 18 and bears striking similarities to the active-site motif recently described in the structure of human PTP1B. The structure of the low-molecular-weight PTPase supports a reaction mechanism involving the conserved Cys 12 as an attacking nucleophile in an in-line associative mechanism. The structure also suggests a catalytic role for Asp 129 in the reaction cycle.
About this Structure
1PHR is a Single protein structure of sequence from Bos taurus with as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase., Su XD, Taddei N, Stefani M, Ramponi G, Nordlund P, Nature. 1994 Aug 18;370(6490):575-8. PMID:8052313
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