1c0e
From Proteopedia
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|PDB= 1c0e |SIZE=350|CAPTION= <scene name='initialview01'>1c0e</scene>, resolution 2.20Å | |PDB= 1c0e |SIZE=350|CAPTION= <scene name='initialview01'>1c0e</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1pnt|1PNT]], [[5pnt|5PNT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c0e OCA], [http://www.ebi.ac.uk/pdbsum/1c0e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c0e RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Tabernero, L.]] | [[Category: Tabernero, L.]] | ||
[[Category: Tishmack, P A.]] | [[Category: Tishmack, P A.]] | ||
| - | [[Category: PO4]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: phosphatase dimer]] | [[Category: phosphatase dimer]] | ||
[[Category: tyrosine phosphatase]] | [[Category: tyrosine 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 19:12:02 2008'' |
Revision as of 16:12, 30 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Acid phosphatase, with EC number 3.1.3.2 | ||||||
| Related: | 1PNT, 5PNT
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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