1ptk: Difference between revisions
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<StructureSection load='1ptk' size='340' side='right'caption='[[1ptk]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1ptk' size='340' side='right'caption='[[1ptk]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ptk]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ptk]] 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=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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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'>[ | <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> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PRTK_TRIAL PRTK_TRIAL]] Hydrolyzes keratin at aromatic and hydrophobic residues. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Proteinase|Proteinase]] | *[[Proteinase|Proteinase]] | ||
*[[Proteinase 3D structures|Proteinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:34, 8 September 2021
STUDIES ON THE INHIBITORY ACTION OF MERCURY UPON PROTEINASE KSTUDIES ON THE INHIBITORY ACTION OF MERCURY UPON PROTEINASE K
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 PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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