2h5u | pdb_00002h5u

Crystal structure of laccase from Cerrena maxima at 1.9A resolution

spinqualitylabelsall models 2h5u, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2h5u is a 1 chain structure with sequence from Trametes maxima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU, MAN, NAG NonStd Res: NIY Related: 1kya Activity: Laccase, with EC number 1.10.3.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Laccases are members of the blue multi-copper oxidase family that oxidize substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. Crystals of the laccase from Cerrena maxima have been obtained and X-ray data were collected to 1.9 A resolution using synchrotron radiation. A preliminary analysis shows that the enzyme has the typical laccase structure and several carbohydrate sites have been identified. The carbohydrate chains appear to be involved in stabilization of the intermolecular contacts in the crystal structure, thus promoting the formation of well ordered crystals of the enzyme. Here, the results of an X-ray crystallographic study on the laccase from the fungus Cerrena maxima are reported. Crystals that diffract well to a resolution of at least 1.9 A (R factor = 18.953%; R(free) = 23.835; r.m.s.d. bond lengths, 0.06 A; r.m.s.d. bond angles, 1.07 degrees) have been obtained despite the presence of glycan moieties. The overall spatial organization of C. maxima laccase and the structure of its copper-containing active centre have been determined by the molecular-replacement method using the laccase from Trametes versicolor (Piontek et al., 2002) as a structural template. In addition, four glycan-binding sites were identified and the 1.9 A X-ray data were used to determine the previously unknown primary structure of this protein. The identity (calculated from sequence alignment) between the C. maxima laccase and the T. versicolor laccase is about 87%. Tyr196 and Tyr372 show significant extra density at the ortho positions and this has been interpreted in terms of NO(2) substituents. Purification, crystallization and preliminary X-ray study of the fungal laccase from Cerrena maxima.,Lyashenko AV, Zhukhlistova NE, Gabdoulkhakov AG, Zhukova YN, Voelter W, Zaitsev VN, Bento I, Stepanova EV, Kachalova GS, Koroleva OV, Cherkashyn EA, Tishkov VI, Lamzin VS, Schirwitz K, Morgunova EY, Betzel C, Lindley PF, Mikhailov AM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):954-7. Epub 2006 Sep 19. PMID:17012782 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laccase 3D structures

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