 | Figure 2
Nature Structural Biology
9, 719 - 724 (2002)
Published online: 23 September 2002; | doi:10.1038/nsb848
The Sak polo-box comprises a structural domain sufficient for mitotic subcellular localizationGenie C. Leung, John W. Hudson, Anna Kozarova, Alan Davidson, James W. Dennis
& Frank Sicheri | | | | Figure 2. Structure of the Sak polo domain dimer.
Ribbons (left) and molecular surface representations (right) of the polo domain homodimer viewed a, perpendicular and b, parallel to the two-fold symmetry axis. Secondary structure elements of one or both of the polypeptide chains are labeled. The molecular surface corresponding to hydrophobic side chains (Met, Val, Leu, Ile and Phe) is green and the N- and C-termini are labeled N and C, respectively. The asterisk indicates the position of the Trp 853 side chains. Shown in ball-and-stick model are the side chains of Lys 906 and Asp 868, which form a tight intermolecular salt interaction on each side of the dimer interface (labeled only on the left side of the dimer). The K906R substitution in polo domain 2 is predicted to form a bidentate salt interaction with Asp 868 and an Asp residue substituted for Val 846 in polo domain 1 (modeled in (a), inset). All ribbon diagrams were generated using Ribbons41. The cross-section of the polo domain surface shown in (a) reveals a large semi-enclosed pocket and interfacial cleft. All molecular surfaces were generated using GRASP42. c, Stereo view of the Sak polo domain highlighting representative electron density of the experimental MAD map contoured at 2.0  . Final model is shown in stick representation. This panel was generated using O39.
|
| | | |  |
|
