Crystallographic refinement of lignin peroxidase at 2 A.

The Journal of Biological Chemistry
T L PoulosM H Gold

Abstract

The crystal structure of the major lignin peroxidase isozyme from Phanerocheate chrysosporium has been refined to an R = 0.15 for data between 8 A and 2.03 A. The refined model consists of 2 lignin peroxidase molecules in the asymmetric unit, 2 calcium ions per monomer, 1 glucosamine per monomer N-linked to Asn-257, and 476 water molecules per asymmetric unit. The model exhibits excellent geometry with a root mean square deviation from ideality in bond distances and angles of 0.014 A and 2.9 degrees, respectively. Molecule 1 consists of all 343 residues, while molecule 2 consists of residues 1-341. The overall root mean square deviation in backbone atoms between the 2 molecules in the asymmetric unit is 0.36 A. The refinement at 2.0 A confirms our conclusions based on the partially refined 2.6-A structure (Edwards, S. L., Raag, R., Wariishi, H., Gold, M. H., and Poulos, T. L. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 750-754). The overall fold of lignin peroxidase closely resembles that of cytochrome c peroxidase. A superimposition of alpha-carbons gives a root mean square deviation of 2.65 A between the two peroxidases and 1.66 A for the helices. The active sites also are similar since both contain a proximal histidine heme lig...Continue Reading

Citations

Jun 25, 2014·Proceedings of the National Academy of Sciences of the United States of America·Robert RileyIgor V Grigoriev
Jan 26, 2020·Applied and Environmental Microbiology·Dolores LindeAngel T Martínez
Jul 30, 2008·FEMS Microbiology Reviews·Ri-He PengQuan-Hong Yao

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