5e9n

Steccherinum murashkinskyi laccase at 0.95 resolution

spinqualitylabelsall models 5e9n, resolution 0.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5e9n is a 1 chain structure with sequence from Steccherinum murashkinskyi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.95Å Ligands: CU, NA, NAG, PG6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I1VE66_9APHY Publication Abstract from PubMed Laccases are multicopper oxidases that catalyze oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. The physicochemical and catalytic properties of two new fungal laccases from basidiomycetes Antrodiella faginea (AfL) and Steccherinum murashkinskyi (SmL) with middle redox potential of the T1 copper site were studied. The X-ray structures of AfL and SmL were solved at 1.75A and 0.95A, respectively. The oxidized state of copper ions in the active site was observed in AfL structure, while the mixture of oxidized and reduced states was observed in SmL structure. These oxidized and reduced states relate to the position of copper ions, their coordination, and nature and position of oxygen ligands. Comparative analysis of the T1 site environment of laccases with known structure allowed us to highlight the six types of the secondary coordination sphere of the T1 copper. The solvent accessible surface area of the conservative region of the secondary coordination sphere of the T1 copper correlates with its the redox potential. It was shown that the laccase classification by the structure of the T1 copper secondary coordination sphere is in agreement to ecophysiological behavior of laccase producing fungi. Structure-function study of two new middle-redox potential laccases from basidiomycetes Antrodiella faginea and Steccherinum murashkinskyi.,Glazunova OA, Polyakov KM, Moiseenko KV, Kurzeev SA, Fedorova TV Int J Biol Macromol. 2018 Jun 15;118(Pt A):406-418. doi:, 10.1016/j.ijbiomac.2018.06.038. PMID:29890251 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laccase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA