1c0e: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1c0e.jpg|left|200px]]


{{Structure
==Active Site S19A Mutant of Bovine Heart Phosphotyrosyl Phosphatase==
|PDB= 1c0e |SIZE=350|CAPTION= <scene name='initialview01'>1c0e</scene>, resolution 2.20&Aring;
<StructureSection load='1c0e' size='340' side='right'caption='[[1c0e]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
<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>
|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>
</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>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=[[1pnt|1PNT]], [[5pnt|5PNT]]
</table>
|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>
== 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>


'''ACTIVE SITE S19A MUTANT OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE'''
==See Also==
 
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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 [http://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].
 
==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:[http://www.ncbi.nlm.nih.gov/pubmed/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: hydrolase]]
[[Category: phosphatase dimer]]
[[Category: tyrosine phosphatase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:12:02 2008''