1phr: Difference between revisions
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|PDB= 1phr |SIZE=350|CAPTION= <scene name='initialview01'>1phr</scene>, resolution 2.1Å | |PDB= 1phr |SIZE=350|CAPTION= <scene name='initialview01'>1phr</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1phr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1phr OCA], [http://www.ebi.ac.uk/pdbsum/1phr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1phr RCSB]</span> | |||
}} | }} | ||
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[[Category: Su, X D.]] | [[Category: Su, X D.]] | ||
[[Category: Taddei, N.]] | [[Category: Taddei, N.]] | ||
[[Category: phosphotyrosine protein phosphatase]] | [[Category: phosphotyrosine protein phosphatase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:59:51 2008'' | ||
Revision as of 19:59, 30 March 2008
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| 1phr, resolution 2.1Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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