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=" | [[Image:1c0e.jpg|left|200px]]<br /><applet load="1c0e" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1c0e, resolution 2.20Å" /> | caption="1c0e, resolution 2.20Å" /> | ||
'''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 | 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:// | 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 | [[Category: Etten, R L.Van.]] | ||
[[Category: Evans, B | [[Category: Evans, B N.]] | ||
[[Category: Stauffacher, C | [[Category: Stauffacher, C V.]] | ||
[[Category: Tabernero, L.]] | [[Category: Tabernero, L.]] | ||
[[Category: Tishmack, P | [[Category: Tishmack, P A.]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| Line 24: | Line 24: | ||
[[Category: tyrosine phosphatase]] | [[Category: tyrosine phosphatase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:04 2008'' | ||