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Figure 5
Comparisons of the glycine-rich loop. (a) Superposition of the glycine-rich loops of apo DAPK (beige), DAPK–ADP–Mg2+ (red) and DAPK–AMP-PNP–Mg2+ (blue) and their position relative to the nucleotide. The DAPK–AMP-PNP–Mg2+ loop has the most closed con­formation. Residues 17–28 are shown for simplicity. The calculated r.m.s. deviation over the Cα atoms of residues 20–25 between the apo DAPK structure and the DAPK–AMP-PNP–Mg2+ structure is 1.03 Å and that between the apo DAPK and DAPK–ADP–Mg2+ structures is 0.62 Å. (b) 2FoFc electron-density map at 1.0σ of the glycine-rich loop of DAPK–ADP–Mg2+. One conformation of Gln23 is modeled such that the side chain is within proximity of the β-phosphate (conformation B). (c) 2FoFc electron-density map of the glycine-rich loop of DAPK–AMP-PNP–Mg2+. The side chain of Phe24 in the DAPK–AMP-PNP structure can be modeled in the `open' conformation (B) or a conformationally restricted position (A).

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BIOLOGY
ISSN: 2059-7983
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