This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2pkc
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2pkc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pkc, resolution 1.5Å" /> '''CRYSTAL STRUCTURE OF ...) |
|||
| (14 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2pkc.jpg|left|200px]]<br /><applet load="2pkc" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2pkc, resolution 1.5Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION'''<br /> | ||
| - | == | + | ==CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION== |
| - | Proteinase K from the fungus Tritirachium album Limber binds two Ca2+ | + | <StructureSection load='2pkc' size='340' side='right'caption='[[2pkc]], [[Resolution|resolution]] 1.50Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2pkc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Beauveria_alba Beauveria alba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PKC FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2pkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkc OCA], [https://pdbe.org/2pkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pkc RCSB], [https://www.ebi.ac.uk/pdbsum/2pkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pkc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://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/pk/2pkc_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=2pkc ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Proteinase K from the fungus Tritirachium album Limber binds two Ca2+ ions, one strongly (Ca 1) and the other weakly (Ca 2). Removal of these cations reduces the stability of proteinase K as shown by thermal denaturation, but the proteolytic activity is unchanged. The x-ray structures of native and Ca(2+)-free proteinase K at 1.5-A resolution show that there are no cuts in the polypeptide backbone (i.e. no autolysis), Ca 1 has been replaced by Na+, while Ca 2 has been substituted by a water associated with a larger but locally confined structural change at that site. A small but concerted geometrical shift is transmitted from the Ca 1 site via eight secondary structure elements to the substrate recognition site (Gly100-Tyr104, and Ser132-Gly136) but not to the catalytic triad (Asp39,His69,Ser224). This is accompanied by positional changes of localized waters. | ||
| - | + | Crystal structure of calcium-free proteinase K at 1.5-A resolution.,Muller A, Hinrichs W, Wolf WM, Saenger W J Biol Chem. 1994 Sep 16;269(37):23108-11. PMID:8083213<ref>PMID:8083213</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2pkc" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ==See Also== | |
| + | *[[Proteinase|Proteinase]] | ||
| + | *[[Proteinase 3D structures|Proteinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beauveria alba]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Peptidase K]] | ||
| + | [[Category: Hinrichs, W]] | ||
| + | [[Category: Mueller, A]] | ||
| + | [[Category: Saenger, W]] | ||
| + | [[Category: Wolf, W M]] | ||
Current revision
CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION
| |||||||||||
