6run: Difference between revisions
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==Co-substituted alpha-Keggin bound to Proteinase K solved by EP== | |||
<StructureSection load='6run' size='340' side='right'caption='[[6run]], [[Resolution|resolution]] 1.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6run]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RUN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=WCO:Co-substituted+alpha-Keggin'>WCO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rug|6rug]], [[6ruh|6ruh]], [[6ruk|6ruk]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6run FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6run OCA], [http://pdbe.org/6run PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6run RCSB], [http://www.ebi.ac.uk/pdbsum/6run PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6run ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6run" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Parengyodontium album]] | |||
[[Category: Peptidase K]] | |||
[[Category: Bijelic, A]] | [[Category: Bijelic, A]] | ||
[[Category: Breibeck, J]] | [[Category: Breibeck, J]] | ||
[[Category: Rompel, A]] | [[Category: Rompel, A]] | ||
[[Category: Alpha-keggin]] | |||
[[Category: Complex]] | |||
[[Category: Polyoxometalate]] | |||
[[Category: Protein binding]] | |||
[[Category: Proteinase k]] | |||
Revision as of 20:57, 20 November 2019
Co-substituted alpha-Keggin bound to Proteinase K solved by EPCo-substituted alpha-Keggin bound to Proteinase K solved by EP
Structural highlights
Function[PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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