3prk: Difference between revisions

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-{{Seed}}
-[[Image:3prk.png|left|200px]]
-<!--
+==INHIBITION OF PROTEINASE K BY METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE. AN X-RAY STUDY AT 2.2-ANGSTROMS RESOLUTION==
-The line below this paragraph, containing "STRUCTURE_3prk", creates the "Structure Box" on the page.
+<StructureSection load='3prk' size='340' side='right' caption='[[3prk]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3prk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Beauveria_alba Beauveria alba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PRK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PRK FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
--->
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QE:CHLOROMETHANE'>0QE</scene>, <scene name='pdbligand=ALV:(2S)-2-AMINOPROPANE-1,1-DIOL'>ALV</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
-{{STRUCTURE_3prk|  PDB=3prk  |  SCENE=  }}
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PROK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37998 Beauveria alba])</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3prk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3prk OCA], [http://pdbe.org/3prk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3prk RCSB], [http://www.ebi.ac.uk/pdbsum/3prk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3prk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PRTK_TRIAL PRTK_TRIAL]] 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/pr/3prk_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=3prk ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of the transition state analog complex formed covalently between proteinase K and methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone was determined by x-ray diffraction methods at a resolution of 2.2 A and refined by constrained least squares to an R factor of 19.8% for the 11864 structure amplitudes greater than 1 sigma F. The chloromethyl ketone group is covalently linked with the active site functional groups His69(N epsilon) and Ser224(O gamma). The former has substituted for chlorine and the latter has attacked the carbon of the ketone group, thereby forming the tetrahedral carbon atom of the transition state analog. The peptide part of the inhibitor is in an extended conformation and fills subsites S1 to S5 of the substrate recognition site. Its backbone hydrogens bond with strands 100-104 and 132-136 of the substrate recognition site as the central strand of a three-stranded antiparallel beta-pleated sheet. This sheet formation is associated with a movement by approximately 1 A of strand 100-104 which is probably associated with the insertion of the bulky proline side chain. The methoxysuccinyl group is stacked on the phenolic side chain of Tyr104 that is a part of the bottom of the recognition site. Biochemical studies show that shorter inhibitors of this type are less effective than the longer one, because there are fewer hydrogen bonding and van der Waals/stacking interactions.
-===INHIBITION OF PROTEINASE K BY METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE. AN X-RAY STUDY AT 2.2-ANGSTROMS RESOLUTION===
+Inhibition of proteinase K by methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone. An x-ray study at 2.2-A resolution.,Wolf WM, Bajorath J, Muller A, Raghunathan S, Singh TP, Hinrichs W, Saenger W J Biol Chem. 1991 Sep 15;266(26):17695-9. PMID:1894649<ref>PMID:1894649</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3prk" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_1894649}}, adds the Publication Abstract to the page
+*[[Proteinase|Proteinase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 1894649 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_1894649}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Beauveria alba]]
-PRK is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PRK OCA].
-==Reference==
-Inhibition of proteinase K by methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone. An x-ray study at 2.2-A resolution., Wolf WM, Bajorath J, Muller A, Raghunathan S, Singh TP, Hinrichs W, Saenger W, J Biol Chem. 1991 Sep 15;266(26):17695-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1894649 1894649]
 [[Category: Peptidase K]]
-[[Category: Single protein]]
+[[Category: Bajorath, J]]
-[[Category: Bajorath, J.]]
+[[Category: Hinrichs, W]]
-[[Category: Hinrichs, W.]]
+[[Category: Mueller, A]]
-[[Category: Mueller, A.]]
+[[Category: Raghunathan, S]]
-[[Category: Raghunathan, S.]]
+[[Category: Saenger, W]]
-[[Category: Saenger, W.]]
+[[Category: Singh, T P]]
-[[Category: Singh, T P.]]
+[[Category: Wolf, W M]]
-[[Category: Wolf, W M.]]
+[[Category: Hydrolase-hydrolase inhibitor complex]]
+[[Category: Serine proteinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:03:13 2008''