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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''' | '''ACTIVE SITE S19A MUTANT OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE''' | ||
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[[Category: Tabernero, L.]] | [[Category: Tabernero, L.]] | ||
[[Category: Tishmack, P A.]] | [[Category: Tishmack, P A.]] | ||
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Phosphatase dimer]] |
| - | [[Category: | + | [[Category: Tyrosine phosphatase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:11:12 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:11, 2 May 2008
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 Page seeded by OCA on Fri May 2 12:11:12 2008
