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α1 deletion perturbs the architecture of ApAAP active site.

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posted on 27.04.2012 by Elena Papaleo, Giulia Renzetti, Matteo Tiberti

A–F) Local network of salt bridge interactions mediated by R526 in the wild type ApAAP (A), ApAAP-Δ21 (B), ApAAP-I12A (C), ApAAP-V13A (D), ApAAP-V16A or ApAAP-I19 (E), ApAAP-L20A (F) are shown with different shade of color which are proportional to the persistence of the interaction during dynamics (with the darker colors indicating an higher persistence). G) wild type ApAAP and ApAAP-Δ21 average structures from the simulations are shown in white and blue, respectively. The catalytic residues are indicated by sticks. H–I) Coupled motions of the catalytic triad. The coupled motions which involve the catalytic triad are shown for wild type ApAAP (red sticks, H) and ApAAP-Δ21 (green sticks, I). Catalytic residues are shown as sticks and the α1-helix highlighted in cyan.

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