5ehf

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Laccase from Antrodiella fagineaLaccase from Antrodiella faginea

Structural highlights

5ehf is a 1 chain structure with sequence from Antrodiella faginea. This structure supersedes the now removed PDB entry 5dao. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0M3U1T9_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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Glazunova OA, Polyakov KM, Moiseenko KV, Kurzeev SA, Fedorova TV. Structure-function study of two new middle-redox potential laccases from basidiomycetes Antrodiella faginea and Steccherinum murashkinskyi. Int J Biol Macromol. 2018 Jun 15;118(Pt A):406-418. doi:, 10.1016/j.ijbiomac.2018.06.038. PMID:29890251 doi:http://dx.doi.org/10.1016/j.ijbiomac.2018.06.038

5ehf, resolution 1.75Å

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