1ptk: Difference between revisions

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-[[Image:1ptk.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1ptk", 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_1ptk|  PDB=1ptk  |  SCENE=  }}
-'''STUDIES ON THE INHIBITORY ACTION OF MERCURY UPON PROTEINASE K'''
+==STUDIES ON THE INHIBITORY ACTION OF MERCURY UPON PROTEINASE K==
+<StructureSection load='1ptk' size='340' side='right'caption='[[1ptk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ptk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PTK 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]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=1ptk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ptk OCA], [https://pdbe.org/1ptk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ptk RCSB], [https://www.ebi.ac.uk/pdbsum/1ptk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ptk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues.
+== 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/pt/1ptk_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ptk ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In proteinase K, Cys73 is located "below" the imidazole of the active site His69. In a 2.4-A resolution x-ray crystal structure of the complex formed between the enzyme and HgAc2, two Hg(II) positions are found: a fully occupied site, covalently bound to Cys73 (S gamma), which disrupts the catalytic triad (Asp39-His69-Ser224), and a 2-fold disordered (25 and 35% occupancy), noncovalent complexation to His72, Cys73, and Thr76 of lower affinity. The enzyme is inhibited noncompetitively at low concentrations and competitively above stoichiometric concentrations of Hg(II), but it retains 7% residual activity. This can be rationalized if the molecule is flexible enough to permit transient formation of the catalytic triad. Except for the active site, only minor structural changes are observed upon binding of Hg(II), but the thermal stability is reduced by 4 degrees C.
-==Overview==
+Studies on the inhibitory action of mercury upon proteinase K.,Muller A, Saenger W J Biol Chem. 1993 Dec 15;268(35):26150-4. PMID:8253733<ref>PMID:8253733</ref>
-In proteinase K, Cys73 is located "below" the imidazole of the active site His69. In a 2.4-A resolution x-ray crystal structure of the complex formed between the enzyme and HgAc2, two Hg(II) positions are found: a fully occupied site, covalently bound to Cys73 (S gamma), which disrupts the catalytic triad (Asp39-His69-Ser224), and a 2-fold disordered (25 and 35% occupancy), noncovalent complexation to His72, Cys73, and Thr76 of lower affinity. The enzyme is inhibited noncompetitively at low concentrations and competitively above stoichiometric concentrations of Hg(II), but it retains 7% residual activity. This can be rationalized if the molecule is flexible enough to permit transient formation of the catalytic triad. Except for the active site, only minor structural changes are observed upon binding of Hg(II), but the thermal stability is reduced by 4 degrees C.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-PTK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTK OCA].
+</div>
+<div class="pdbe-citations 1ptk" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Studies on the inhibitory action of mercury upon proteinase K., Muller A, Saenger W, J Biol Chem. 1993 Dec 15;268(35):26150-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8253733 8253733]
+*[[Proteinase 3D structures|Proteinase 3D structures]]
-[[Category: Engyodontium album]]
+== References ==
-[[Category: Peptidase K]]
+<references/>
-[[Category: Single protein]]
+__TOC__
-[[Category: Mueller, A.]]
+</StructureSection>
-[[Category: Saenger, W.]]
+[[Category: Large Structures]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:28:16 2008''
+[[Category: Parengyodontium album]]
+[[Category: Mueller A]]
+[[Category: Saenger W]]