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2pkc

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[[Image:2pkc.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION==
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|PDB= 2pkc |SIZE=350|CAPTION= <scene name='initialview01'>2pkc</scene>, resolution 1.5&Aring;
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<StructureSection load='2pkc' size='340' side='right'caption='[[2pkc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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<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>
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|ACTIVITY= [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]
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</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>
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|GENE=
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<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>
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}}
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<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>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/PRTK_TRIAL PRTK_TRIAL]] Hydrolyzes keratin at aromatic and hydrophobic residues.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pk/2pkc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2pkc" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Proteinase|Proteinase]]
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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==About this Structure==
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== References ==
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2PKC 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=2PKC OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8083213 8083213]
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[[Category: Beauveria alba]]
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[[Category: Engyodontium album]]
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[[Category: Large Structures]]
[[Category: Peptidase K]]
[[Category: Peptidase K]]
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[[Category: Single protein]]
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[[Category: Hinrichs, W]]
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[[Category: Hinrichs, W.]]
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[[Category: Mueller, A]]
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[[Category: Mueller, A.]]
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[[Category: Saenger, W]]
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[[Category: Saenger, W.]]
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[[Category: Wolf, W M]]
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[[Category: Wolf, W M.]]
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[[Category: NA]]
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[[Category: hydrolase(serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:14:04 2008''
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Current revision

CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION

PDB ID 2pkc

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