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Figure 1.
Structure of YxiN(207 --368). (a) Ribbon diagram of protomer
A. [beta]-Strands and selected [alpha]-helices are numbered
sequentially. The motif V and VI loops are labeled. (b)
Superposition of the two protomers in the asymmetric unit. A
stereo diagram of the C[[alpha]] trace is shown as a smoothed
coil. The backbones of segments of peptide where C[[alpha]]
positions differ by <0.5 A are shown in yellow for both
protomers; segments where C[[alpha]] positions differ by >0.5 A
are shown in magenta (protomer A) and cyan (protomer B). The
side chains of selected residues of helicase motifs V and VI, as
well as Asp298, are shown for protomer A. The orientation of the
figure is rotated approximately 180[deg] around a vertical axis
relative to the schematic drawing in (a). (c) Crystal-packing
interactions involving residues from motifs V and VI. Only the
side chains of residues from motifs V and VI that are involved
in intermolecular interactions are shown. Protomer A, red;
protomer B, blue; symmetry-related A, magenta; symmetry-related
B, cyan. All figures were produced using PyMOL
(http://www.pymol.org). Acta Crystallogr Sect F Struct Biol
Cryst Commun. 2006 December 1; 62(Pt 12): 1191–1195. Published
online 2006 November 30. doi: 10.1107/S1744309106044642.
Copyright [copyright] International Union of Crystallography
2006
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