1v73: Difference between revisions

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-[[Image:1v73.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1v73", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1v73|  PDB=1v73  |  SCENE=  }}
-'''Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase of a Psychrophile Shewanella SP.'''
+==Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase of a Psychrophile Shewanella SP.==
+<StructureSection load='1v73' size='340' side='right'caption='[[1v73]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1v73]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_sp. Shewanella sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V73 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V73 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]] 1.82&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1v73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v73 OCA], [https://pdbe.org/1v73 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v73 RCSB], [https://www.ebi.ac.uk/pdbsum/1v73 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v73 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9S427_9GAMM Q9S427_9GAMM]
+== 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/v7/1v73_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=1v73 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The cold-active protein-tyrosine phosphatase (CAPTPase) of a psychrophile, Shewanella sp., shows high catalytic activity below 20 degrees C. The catalytic residue of CAPTPase is histidine, as opposed to the cysteine of known protein-tyrosine phosphatases (PTPases), and the enzyme protein has three amino acid sequences, Asp-Xaa-His, Gly-Asp-Xaa-Xaa-Asp-Arg and Gly-Asn-His-Glu, that are observed in many protein-serine/threonine phosphatases (PS/TPases). We have determined the crystal structures of CAPTPase at 1.82 angstroms and the enzyme bound with a phosphate ion at 1.90 angstroms resolution using X-ray crystallography and the multiple isomorphous replacement method. The final refined models are comprised of 331 amino acid residues, two metal ions, 447 water molecules, and an acetate or phosphate ion in an asymmetric unit. The enzyme protein consists of three beta-sheets, termed Sheet I, Sheet I', and Sheet II, and 14 alpha-helices. The CAPTPase has a different overall structure from known protein-tyrosine phosphatases. The arrangement of two metal ions, a phosphate ion and the adjacent amino acid residues in the catalytic site of CAPTPase is identical to that of PS/TPases. Thus, it was confirmed that the CAPTPase was a novel PTPase with a conformation similar to the catalytic site of PS/TPase. We speculate that the hydrophobic moiety around the catalytic residue of CAPTPase might play an important role in eliciting high activity at low temperature.
-==Overview==
+Crystal structure of cold-active protein-tyrosine phosphatase from a psychrophile, Shewanella sp.,Tsuruta H, Mikami B, Aizono Y J Biochem. 2005 Jan;137(1):69-77. PMID:15713885<ref>PMID:15713885</ref>
-The cold-active protein-tyrosine phosphatase (CAPTPase) of a psychrophile, Shewanella sp., shows high catalytic activity below 20 degrees C. The catalytic residue of CAPTPase is histidine, as opposed to the cysteine of known protein-tyrosine phosphatases (PTPases), and the enzyme protein has three amino acid sequences, Asp-Xaa-His, Gly-Asp-Xaa-Xaa-Asp-Arg and Gly-Asn-His-Glu, that are observed in many protein-serine/threonine phosphatases (PS/TPases). We have determined the crystal structures of CAPTPase at 1.82 angstroms and the enzyme bound with a phosphate ion at 1.90 angstroms resolution using X-ray crystallography and the multiple isomorphous replacement method. The final refined models are comprised of 331 amino acid residues, two metal ions, 447 water molecules, and an acetate or phosphate ion in an asymmetric unit. The enzyme protein consists of three beta-sheets, termed Sheet I, Sheet I', and Sheet II, and 14 alpha-helices. The CAPTPase has a different overall structure from known protein-tyrosine phosphatases. The arrangement of two metal ions, a phosphate ion and the adjacent amino acid residues in the catalytic site of CAPTPase is identical to that of PS/TPases. Thus, it was confirmed that the CAPTPase was a novel PTPase with a conformation similar to the catalytic site of PS/TPase. We speculate that the hydrophobic moiety around the catalytic residue of CAPTPase might play an important role in eliciting high activity at low temperature.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-V73 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_sp. Shewanella sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V73 OCA].
+</div>
+<div class="pdbe-citations 1v73" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Crystal structure of cold-active protein-tyrosine phosphatase from a psychrophile, Shewanella sp., Tsuruta H, Mikami B, Aizono Y, J Biochem. 2005 Jan;137(1):69-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15713885 15713885]
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
-[[Category: Protein-tyrosine-phosphatase]]
+== References ==
-[[Category: Shewanella sp.]]
+<references/>
-[[Category: Single protein]]
+__TOC__
-[[Category: Aizono, Y.]]
+</StructureSection>
-[[Category: Mikami, B.]]
+[[Category: Large Structures]]
-[[Category: Tsuruta, H.]]
-[[Category: Cold-active enzyme]]
-[[Category: Protein-tyrosine phosphatase]]
-[[Category: Psychrophile]]
 [[Category: Shewanella sp]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:10:18 2008''
+[[Category: Aizono Y]]
+[[Category: Mikami B]]
+[[Category: Tsuruta H]]