1c0e
From Proteopedia
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| - | [[Image:1c0e.jpg|left|200px]] | + | [[Image:1c0e.jpg|left|200px]] |
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| - | '''ACTIVE SITE S19A MUTANT OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE''' | + | {{Structure |
| + | |PDB= 1c0e |SIZE=350|CAPTION= <scene name='initialview01'>1c0e</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ACTIVE SITE S19A MUTANT OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C0E is a [ | + | 1C0E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C0E OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism., Tabernero L, Evans BN, Tishmack PA, Van Etten RL, Stauffacher CV, Biochemistry. 1999 Sep 7;38(36):11651-8. PMID:[http:// | + | The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism., Tabernero L, Evans BN, Tishmack PA, Van Etten RL, Stauffacher CV, Biochemistry. 1999 Sep 7;38(36):11651-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10512620 10512620] |
[[Category: Acid phosphatase]] | [[Category: Acid phosphatase]] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
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[[Category: tyrosine phosphatase]] | [[Category: tyrosine phosphatase]] | ||
| - | ''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 10:18:17 2008'' |
Revision as of 08:18, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | |||||||
| Activity: | Acid phosphatase, with EC number 3.1.3.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ACTIVE SITE S19A MUTANT OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE
Overview
The bovine protein tyrosine phosphatase (BPTP) is a member of the class of low-molecular weight protein tyrosine phosphatases (PTPases) found to be ubiquitous in mammalian cells. The catalytic site of BPTP contains a CX(5)R(S/T) phosphate-binding motif or P-loop (residues 12-19) which is the signature sequence for all PTPases. Ser19, the final residue of the P-loop motif, interacts with the catalytic Cys12 and participates in stabilizing the conformation of the active site through interactions with Asn15, also in the P-loop. Mutations at Ser19 result in an enzyme with altered kinetic properties with changes in the pK(a) of the neighboring His72. The X-ray structure of the S19A mutant enzyme shows that the general conformation of the P-loop is preserved. However, changes in the loop containing His72 result in a displacement of the His72 side chain that may explain the shift in the pK(a). In addition, it was found that in the crystal, the protein forms a dimer in which Tyr131 and Tyr132 from one monomer insert into the active site of the other monomer, suggesting a dual-tyrosine motif on target sites for this enzyme. Since the activity of this PTPase is reportedly regulated by phosphorylation at Tyr131 and Tyr132, the structure of this dimer may provide a model of a self-regulation mechanism for the low-molecular weight PTPases.
About this Structure
1C0E is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism., Tabernero L, Evans BN, Tishmack PA, Van Etten RL, Stauffacher CV, Biochemistry. 1999 Sep 7;38(36):11651-8. PMID:10512620
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