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![[Figure 5]](hm5071fig5mag.jpg)
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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) 2Fo − Fc 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) 2Fo − Fc 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). |
![[Figure 5]](hm5071fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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