Supplementary Figure 10: Proposed network effect model explaining the quantitative behavior of the indicated cross-links. | Nature Methods

Supplementary Figure 10: Proposed network effect model explaining the quantitative behavior of the indicated cross-links.

From: xTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometry

Supplementary Figure 10

(a) and (b): Stereo view of the active site of luciferase with bound DLSA in two different conformations (PDB ID 4G36 and 4G37). The residues Lys529 and Lys443 which contact the substrate are indicated by arrows. Adapted with permission from Sundlov, J. A., Fontaine, D. M., Southworth, T. L., Branchini, B. R. & Gulick, A. M. (2012). Biochemistry 51, 6493-6495. Copyright 2012 American Chemical Society. (c) Proposed model suggesting that inhibition of the formation of the cross-link between Lys142 and Lys529, which is blocked by the substrate binding, leads to the dominant cross-link 142-541 which shows a twofold increase in the second conformation. At the same time the cross-links 142-380 and 142-329 show a decreased abundance in the second confirmation presumably due to the dominant cross-link 142-541 and structural rearrangements.

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