4ako | pdb_00004ako

Mutations in the neighbourhood of CotA-laccase trinuclear site: E498L mutant

spinqualitylabelsall models 4ako, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ako is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU, EDO, OXY NonStd Res: CSX Related: 1gsk, 1of0, 1uvw, 1w6l, 1w6w, 1w8e, 2bhf, 2x87, 2x88, 4a66, 4a67, 4a68, 4akp, 4akq Activity: Laccase, with EC number 1.10.3.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [COTA_BACSU] Involved in brown pigmentation during sporogenesis. Publication Abstract from PubMed The multicopper oxidases couple the one-electron oxidation of four substrate molecules to the four electron reductive cleavage of the O-O bond of dioxygen. This reduction takes place at the trinuclear copper centre of the enzyme and the dioxygen approaches this centre through an entrance channel. In this channel, an acidic residue plays a key role in steering the dioxygen to the trinuclear copper site, providing protons for the catalytic reaction and giving overall stability to this site. In this study, the role of the Glu(498) residue, located within the entrance channel to the trinuclear copper centre, has been investigated in the binding and reduction of dioxygen by the CotA-laccase from Bacillus subtilis. The absence of an acidic group at the 498 residue, as in the E498T and E498L mutants, results in a severe catalytic impairment, higher than 99%, for the phenolic and non-phenolic substrates tested. The replacement of this glutamate by aspartate leads to an activity that is around 10% relative to that of the wild-type. Furthermore, while this latter mutant shows a similar K(m) value for dioxygen, the E498T and E498L mutants show a decreased affinity, when compared to the wild-type. X-ray structural and spectroscopic analysis (UV-visible, electron paramagnetic resonance and resonance Raman) reveal perturbations of the structural properties of the catalytic centres in the Glu(498) mutants when compared to the wild-type protein. Overall, the results strongly suggest that Glu(498) plays a key role in the protonation events that occur at the trinuclear centre and in its stabilization, controlling therefore the binding of dioxygen and its further reduction. The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis.,Chen Z, Durao P, Silva CS, Pereira MM, Todorovic S, Hildebrandt P, Bento I, Lindley PF, Martins LO Dalton Trans. 2010 Mar 21;39(11):2875-82. Epub 2010 Feb 5. PMID:20200715 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laccase 3D structures

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