View source for 6ruh


==Ni-substituted alpha-Keggin bound to Proteinase K solved by MR==
<StructureSection load='6ruh' size='340' side='right'caption='[[6ruh]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ruh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RUH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=WNI:Ni-substituted+alpha-Keggin'>WNI</scene></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=6ruh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ruh OCA], [https://pdbe.org/6ruh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ruh RCSB], [https://www.ebi.ac.uk/pdbsum/6ruh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ruh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The use of alpha- and beta-Keggin polyoxotungstates (POTs) substituted by a single first row transition metal ion (CoII, NiII, CuII, ZnII) as superchaotropic crystallization additives led to covalent and non-covalent interactions with protein side-chains of proteinase K. Two major Keggin POT binding sites in proteinase K were identified, both stabilizing the orientation of the substituted metal site towards the protein surface and suggesting increased protein affinity for the substitution sites. The formation of all observed covalent bonds involves the same aspartate carboxylate, taking the role of a terminal oxygen with the Keggin alpha-isomer or even, in an unprecedented scenario, a bridging cluster oxygen with the beta-isomer. Covalent bond formation with the protein carboxylate was observed only with the NiII- and CoII-substituted POTs, following the HSAB concept and the principle of metal immobilization.

Transition metal-substituted Keggin polyoxotungstates enabling covalent attachment to proteinase K upon co-crystallization.,Breibeck J, Bijelic A, Rompel A Chem Commun (Camb). 2019 Sep 24;55(77):11519-11522. doi: 10.1039/c9cc05818d. PMID:31490500<ref>PMID:31490500</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ruh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Parengyodontium album]]
[[Category: Bijelic A]]
[[Category: Breibeck J]]
[[Category: Rompel A]]