Appendix A. Details of the identification and selection of studies and statistical analyses used to determine if exotic herbivores are better competitors.

Details of the identification and selection of studies and statistical analyses used to determine if exotic herbivores are better competitors

Supplement 1. List of all competing insect pairs evaluated and the number of times they were used in the database.

<h2>File List</h2><div> <p><a href="supplement.txt">supplement.txt</a> (MD5: 2cba90e4b399577ead043507d4c87d39) </p> </div><h2>Description</h2><div> List of all competing insect pairs evaluated and the number of times they were used in the database.</div

Appendix B. Analyses of the importance of coevolutionary history, temporal separation, and spatial separation on interspecific competition when controlling exotic/native status of the focal and competing herbivore.

Analyses of the importance of coevolutionary history, temporal separation, and spatial separation on interspecific competition when controlling exotic/native status of the focal and competing herbivore

MOESM1 of Structural and functional characterization of a highly stable endo-β-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst

Additional file 1. Additional Fig. 1. Schematic representation of Xyl2 topology. Additional Fig. 2. Docking of a xylose hexaoligosaccharide on Xyl2 (pH 5). Additional Fig. 3. Schematic representation of the rationale for random enzyme immobilization via the carrier or carrier-free approaches. Negative correlation between Xyl2 activity yield and functionalization degree in high and low agarose supports. Additional Table 1. Guiding values for binding capacities of commercial agarose beads employed for Xyl2 immobilization

Structural comparison of CsdE along the proposed conformational change.

<p>(A) Superposition in cartoon with helices shown as cylinders of the CsdE free monomer from X-Ray (overlaid structures colored in green, white and red to highlight the movement, with the Cys61 Cα atom represented as a sphere), the CsdE monomer of dimer of the present study (pale blue) and CsdE monomer from the X-Ray structure of the (CsdA-CsdE)₂ complex (cyan). The CsdE free monomer is depicted over the ensemble-weighted maximally correlated mode contributing to the change in the selected distance (d[Cys61(Cα)–Val88(Cα)]). (B) Insight of the CsdE free monomer’s movement of the loop is shown with Cys61 side chain represented as balls and sticks.</p

Crystal structure of the CsdE dimer.

<p>(A) Top (left) and side (right) views of the disulfide-bridged CsdE dimer, shown in cartoon representation with the two chains in cyan and slate blue colors. Cys61 side chain and the disulfide bridge between them is represented in sticks, with the sulfur atoms in yellow and the carbon atoms in chain colors. (B) Zoom-in into the disulfide bridge holding together the CsdE dimer. The electron density map is a σ_A-weighted 2<i>DF</i>_O−<i>mF</i>_C map contoured at 1.2 σ in grey. (C) Angle between the vectors joining the center-of-mass of the disulfide bridge and those of monomers of the CsdE dimer during the simulation. The red line indicates the value determined from the X-ray structure.</p

Distance between the Cα atoms of Cys61 and Val88 during the MD simulation of the CsdE monomer in solution with an anionic Cys61.

<p>Representative structures over the MD simulation are depicted, where the protein is colored in green for the buried conformation of Cys61 and in red for the solvent exposed conformation, Cys61 residue side chain is represented with balls.</p

Cys61 as an interface hub on CsdE exposed surface.

<p>(A) Opaque molecular surfaces of CsdE (white) with the position of Cys61 mapped out in yellow. From the top right corner and following a clockwise rotation, the following interaction surfaces are shown: TcdA (in pink), CsdA (persulfurated complex, in green), the two non-symmetric CsdE interaction surfaces (in cyan and in blue slate). (B) Close-up on the molecular surface of CsdE around Cys61 (yellow; labeled C61). The outlines of the interaction surfaces shown in (A) are drawn in thick line with the same color code; each area is labeled with the protein that occupies the respective surface area.</p

Functional consequences of CsdE inactivation by disulfide bridge formation.

<p>A functional CsdA-CsdE sulfur mobilization system is depicted inside a cyan outline. CsdA, CsdE, and TcdA are represented as molecular surfaces. The tRNA molecules in the TcdA-tRNA complex are bead models derived from SAXS [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0186286#pone.0186286.ref041" target="_blank">41</a>]. CsdE is color coded in light cyan (CsdA unbound form) or bright cyan (bound to CsdA). CsdA subunits are colored in green and violet. TcdA subunits are shown in pale green and wheat. The tRNA bead models are in yellow. The inactivation of CsdE during oxidative stress conditions would likely lead to the impairment of the CsdA-CsdE downstream effector functions, the best known of which is the effect on ribosomal translation efficiency and fidelity through the TcdA-tRNA^ANN complex.</p

Interaction network at the CsdE dimer interface.

<p>(A) The two CsdE monomers are shown in ribbon representation. Cys61 side-chain atoms are shown in yellow to mark its position with respect to the monomer-monomer interfaces. The structural elements of each monomer contacted by the opposite monomer are shown mapped in slate blue (top) or cyan (below). (B) Close-up around the disulfide bridge depicting the details of the interaction network that consolidates the dimer. Helices α7 are labeled H7 and β-strands β1, β2, and β3 are labeled as B1, B2, and B3, respectively, only in the top monomer (cyan). Cys61 is harbored in the small loop connecting β2 and β3. Interacting amino acid residues are represented in sticks (main and side chains) and the interactions are depicted by black dashed lines.</p