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==Proteinase K by LB nanotemplate method after the fourth step of high X-Ray dose on ESRF ID23-1 beamline== | |||
<StructureSection load='3de2' size='340' side='right'caption='[[3de2]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3de2]] is a 1 chain structure with 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=3DE2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3DE2 FirstGlance]. <br> | |||
</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></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d9q|3d9q]], [[3ddz|3ddz]], [[3de0|3de0]], [[3de1|3de1]], [[3de3|3de3]], [[3de4|3de4]], [[3de5|3de5]], [[3de6|3de6]], [[3de7|3de7]]</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://proteopedia.org/fgij/fg.htm?mol=3de2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3de2 OCA], [http://pdbe.org/3de2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3de2 RCSB], [http://www.ebi.ac.uk/pdbsum/3de2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3de2 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/de/3de2_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=3de2 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A detailed analysis of structural and intensity changes induced by X-ray radiation is presented for two types of proteinase K crystals: crystal grown by classical hanging drop method and those grown by Langmuir-Blodgett (LB) nanotemplate. The comparison of various parameters (e.g. intensity per sigma ratio, unit-cell volume, number of unique reflections, B-factors) and electron density maps as a function of radiation dose, demonstrates that crystals, grown by the LB nanotemplate method, appear to be more resistant against radiation damage than crystals grown by the classical hanging drop method. | |||
Radiation stability of proteinase K crystals grown by LB nanotemplate method.,Pechkova E, Tripathi S, Ravelli RB, McSweeney S, Nicolini C J Struct Biol. 2009 Dec;168(3):409-18. Epub 2009 Aug 15. PMID:19686853<ref>PMID:19686853</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3de2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Proteinase|Proteinase]] | |||
*[[Proteinase 3D structures|Proteinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Engyodontium album]] | |||
[[Category: Large Structures]] | |||
[[Category: Peptidase K]] | |||
[[Category: Nicolini, C]] | |||
[[Category: Pechkova, E]] | |||
[[Category: Tripathi, S K]] | |||
[[Category: Alpha and beta protein]] | |||
[[Category: Calcium]] | |||
[[Category: Hydrolase]] | |||
[[Category: Metal-binding]] | |||
[[Category: Protease]] | |||
[[Category: Serine protease]] | |||
[[Category: Zymogen]] | |||
Latest revision as of 09:58, 19 August 2020
Proteinase K by LB nanotemplate method after the fourth step of high X-Ray dose on ESRF ID23-1 beamlineProteinase K by LB nanotemplate method after the fourth step of high X-Ray dose on ESRF ID23-1 beamline
Structural highlights
Function[PRTK_TRIAL] Hydrolyzes keratin at aromatic and hydrophobic residues. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA detailed analysis of structural and intensity changes induced by X-ray radiation is presented for two types of proteinase K crystals: crystal grown by classical hanging drop method and those grown by Langmuir-Blodgett (LB) nanotemplate. The comparison of various parameters (e.g. intensity per sigma ratio, unit-cell volume, number of unique reflections, B-factors) and electron density maps as a function of radiation dose, demonstrates that crystals, grown by the LB nanotemplate method, appear to be more resistant against radiation damage than crystals grown by the classical hanging drop method. Radiation stability of proteinase K crystals grown by LB nanotemplate method.,Pechkova E, Tripathi S, Ravelli RB, McSweeney S, Nicolini C J Struct Biol. 2009 Dec;168(3):409-18. Epub 2009 Aug 15. PMID:19686853[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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