A Mimivirus Enzyme that Participates in Viral Entry Thomas Klose, Dominik A. Herbst, Hanyu Zhu, Joann P. Max, Hilkka I. Kenttämaa, Michael G. Rossmann  Structure  Volume 23, Issue 6, Pages 1058-1065 (June 2015) DOI: 10.1016/j.str.2015.03.023 Copyright © 2015 Elsevier Ltd Terms and Conditions

Structure 2015 23, 1058-1065DOI: (10.1016/j.str.2015.03.023) Copyright © 2015 Elsevier Ltd Terms and Conditions

Figure 1 Structure of R135 (A and B) Top view (A) and side view (B) of an R135 dimer, rainbow colored from blue at the N terminus to red at the C terminus. (C and D) Top view (C) and side view (D) of an R135 dimer. Each monomer is colored in red and green, respectively. Structure 2015 23, 1058-1065DOI: (10.1016/j.str.2015.03.023) Copyright © 2015 Elsevier Ltd Terms and Conditions

Figure 2 Topology Diagram of R135 The FAD binding domain and the substrate recognition domain are colored in green and blue, respectively, and are separated by a black line. The FAD binding loop involved in dimer formation is shown in orange. Structure 2015 23, 1058-1065DOI: (10.1016/j.str.2015.03.023) Copyright © 2015 Elsevier Ltd Terms and Conditions

Figure 3 Oligomer Formation of R135 in Solution Analyzed by Sedimentation Velocity Centrifugation The majority of R135 forms a dimer with a sedimentation coefficient of 7.8 S in solution, independent of the protein concentration. Structure 2015 23, 1058-1065DOI: (10.1016/j.str.2015.03.023) Copyright © 2015 Elsevier Ltd Terms and Conditions

Figure 4 FAD Cofactor and its Protein Environment Shown are the residues involved in hydrogen bonds (depicted by dashed lines) and hydrophobic interactions with the flavin ligand. The figure was generated using the program LIGPLOT+ (Laskowski and Swindells, 2011). Structure 2015 23, 1058-1065DOI: (10.1016/j.str.2015.03.023) Copyright © 2015 Elsevier Ltd Terms and Conditions

Figure 5 Electron Density Surrounding the FAD Cofactor (A and B) Model of the FAD cofactor shown from the top (A) and side (B). The 2Fo − Fc electron density map drawn at a σ level of 1.0 is shown as a mesh. (C and D) Overlays of a planar (red) and the observed butterfly (green) conformation shown from the top (C) and side (D). The electron density map is displayed in the same way as in (A) and (B). Structure 2015 23, 1058-1065DOI: (10.1016/j.str.2015.03.023) Copyright © 2015 Elsevier Ltd Terms and Conditions

Figure 6 Lignin Model Dimer Chemical structure of guaiacylglycerol-β-guaiacyl ether, the compound used in all lignin degradation assays. Structure 2015 23, 1058-1065DOI: (10.1016/j.str.2015.03.023) Copyright © 2015 Elsevier Ltd Terms and Conditions