 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 6]](mn5019fig6mag.jpg)
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Figure 6
Crystal structure of oxidized Nm23-H1. (a) Superposition of monomers of the oxidized and native forms. The native form is coloured cyan. The oxidized form is coloured green, with the K-pn loop region in white, helix H7 (linker helix) in scarlet and the C-terminal domain in yellow. Some of the secondary-structural elements are labelled in blue for the native form and in black for the oxidized form. The phosphate ion and the residues Lys12 and His118 that are essential for NDPK activity form salt bridges with distances of 3.03 and 2.72 Å, respectively. His118, Ser120 and Glu129 form a hydrogen-bond network essential for anchoring the C-terminal domain to the core domain. The distances of the hydrogen bonds His118 N∊2⋯Glu129 O∊1, His118 N∊2⋯Glu129 O∊2 and Ser120 Oγ⋯Glu129 O∊1 are 3.01, 3.15 and 2.60 Å, respectively. The residues that interact with ADP are represented and labelled. Gly113 is marked with an asterisk. (b) Oxidized (left) and native (right) Nm23-H1 hexamers in crystals. The cysteine residues are represented by spheres: orange for Cys4, cyan for Cys109 and yellow for Cys145. The sulfate molecules are represented as ball-and-stick models. (c) This figure was obtained by rotating (b) through 90° along the x axis. |
![[Figure 6]](mn5019fig6.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
