Interaction of extended loop 882-892 of Cp with Mpo.

<p>Cp is shown in blue, heavy chain of Mpo in palegreen, light chain of Mpo in pink. Copper ions are shown as orange spheres. Heme is shown in violet, ferrous is shown in gray sphere. (<b>A</b>) Overall view of Cp monomer contact with Mpo monomer. Selected contact is indicated by dash-line oval (<b>B</b>). Zoom of contact area of Cp with the entrance of heme pocket of Mpo. Cp is shown in cartoon; Mpo is shown in cartoon and semi-transparent surface representation. Ends of loop between domain 5 and 6 are marked. <b>(C)</b> Inhibition of ABTS-peroxidase activity of Mpo by synthetic peptide RPYLKVFNPR corresponding to the 883-892 fragment of Cp sequence.</p

Data collection statistics and refinement for Cp-Mpo complex and Cp with free labile sites.

*<p>Values in parentheses are for highest resolution shell.</p

Cp-Mpo-Lf in solution.

<p>(<b>A</b>) Scattering patterns of ternary complex and individual proteins. (1): Mpo dimer, (2) Cp with glycans, (3) glycosylated Lf, (4) Monomeric binary complex Cp-Lf and (5) ternary complex. Experimental data are denoted by dots, fits computed from the appropriate portions of the SAXS model are shown as red solid lines. The plots are displaced along the logarithmic scale for better visualization. Insert: Guinier plots (ln I <i>versus</i> s²) with the linear fits (straight lines) in the ranges automatically determined by AutoRg (Petoukhov et al., 2012). (<b>B</b>) SAXS models of the ternary complex. Rigid body model is presented by Ca trace whereby Cp and Lf subunits (two copies each) and Mpo dimer are shown in red, blue and green, respectively. The location of sugars is denoted by appropriately colored solid spheres. Bottom view is rotated by 90 degrees around horizontal axis. <i>Ab initio</i> shapes of the ternary complex (top) reconstructed in P2 and of Cp-Lf (bottom) are shown as grey beads. (<b>C</b>) Zoom of Cp-Lf interaction in ribbon and transparent surface representation. One of possible Lf sugar chain conformation (brown sticks and pink semitransparent surface) is shown in stick and surface representation. Lf-N1 is shown in chocolate, Lf-N2 in yellow, Lf-C1 in pink and Lf-C2 in red. Cp is shown in light cyan. Border of domain 1 is highlighted by blue line. Glycosylation site N119 indicates by black arrow.</p