1c0e: Difference between revisions

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New page: left|200px<br /><applet load="1c0e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c0e, resolution 2.20Å" /> '''ACTIVE SITE S19A MUT...
 
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[[Image:1c0e.jpg|left|200px]]<br /><applet load="1c0e" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1c0e.jpg|left|200px]]<br /><applet load="1c0e" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1c0e, resolution 2.20&Aring;" />
caption="1c0e, resolution 2.20&Aring;" />
'''ACTIVE SITE S19A MUTANT OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE'''<br />
'''ACTIVE SITE S19A MUTANT OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE'''<br />


==Overview==
==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.
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==
==About this Structure==
1C0E 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C0E OCA].  
1C0E 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=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C0E OCA].  


==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Etten, R.L.Van.]]
[[Category: Etten, R L.Van.]]
[[Category: Evans, B.N.]]
[[Category: Evans, B N.]]
[[Category: Stauffacher, C.V.]]
[[Category: Stauffacher, C V.]]
[[Category: Tabernero, L.]]
[[Category: Tabernero, L.]]
[[Category: Tishmack, P.A.]]
[[Category: Tishmack, P A.]]
[[Category: PO4]]
[[Category: PO4]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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[[Category: tyrosine phosphatase]]
[[Category: tyrosine phosphatase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:03:45 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:04 2008''