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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"
caption="1c0e, resolution 2.20&Aring;" />
'''ACTIVE SITE S19A MUTANT OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE'''<br />


==Overview==
==Active Site S19A Mutant of Bovine Heart Phosphotyrosyl Phosphatase==
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.
<StructureSection load='1c0e' size='340' side='right'caption='[[1c0e]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1c0e]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C0E FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c0e OCA], [https://pdbe.org/1c0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c0e RCSB], [https://www.ebi.ac.uk/pdbsum/1c0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c0e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPAC_BOVIN PPAC_BOVIN] Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c0/1c0e_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c0e ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10512620 10512620]
[[Category: Acid phosphatase]]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Etten, R.L.Van.]]
[[Category: Evans BN]]
[[Category: Evans, B.N.]]
[[Category: Stauffacher CV]]
[[Category: Stauffacher, C.V.]]
[[Category: Tabernero L]]
[[Category: Tabernero, L.]]
[[Category: Tishmack PA]]
[[Category: Tishmack, P.A.]]
[[Category: Van Etten RL]]
[[Category: PO4]]
[[Category: hydrolase]]
[[Category: phosphatase dimer]]
[[Category: tyrosine phosphatase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:03:45 2007''

Latest revision as of 06:40, 7 February 2024

Active Site S19A Mutant of Bovine Heart Phosphotyrosyl Phosphatase

1c0e, resolution 2.20Å

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