6zip

Crystal Structure of Two-Domain Laccase mutant R240A from Streptomyces griseoflavus

spinqualitylabelsall models 6zip, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zip is a 12 chain structure with sequence from Streptomyces griseoflavus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: CU, GOL, OXY, PER Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M4FJ81_9ACTN Publication Abstract from PubMed Multi-copper oxidases are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. This process takes place at the trinuclear copper center of the enzymes. Previously, the main catalytic stages for three-domain (3D) laccases have been identified. However, for bacterial small two-domain (2D) laccases several questions remain to be answered. One of them is the nature of the protonation events upon the reductive cleavage of dioxygen to water. In 3D laccases, acidic residues play a key role in the protonation mechanisms. In this study, the role of the Arg240 residue, located within the T2 tunnel of 2D laccase from Streptomyces griseoflavus Ac-993, was investigated. X-ray structural analysis and kinetic characterization of two mutants, R240A and R240H, have provided support for a role of this residue in the protonation events. Communicated by Ramaswamy H. Sarma. The role of positive charged residue in the proton-transfer mechanism of two-domain laccase from Streptomyces griseoflavus Ac-993.,Gabdulkhakov A, Kolyadenko I, Oliveira P, Tamagnini P, Mikhaylina A, Tishchenko S J Biomol Struct Dyn. 2021 Apr 19:1-8. doi: 10.1080/07391102.2021.1911852. PMID:33870857 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laccase 3D structures

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