6ruh

Ni-substituted alpha-Keggin bound to Proteinase K solved by MR

spinqualitylabelsall models 6ruh, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ruh is a 1 chain structure with sequence from Parengyodontium album. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.1Å Ligands: SO4, WNI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRTK_PARAQ Hydrolyzes keratin at aromatic and hydrophobic residues. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proteinase 3D structures

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