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. 2014 Feb 11;289(13):8960–8972. doi: 10.1074/jbc.M113.536557

FIGURE 1.

FIGURE 1.

Comparison of PII structures from S. elongatus in the absence of cofactors. All structures are shown as schematics prepared using PyMOL. A, superposition of the two wild-type structures PIINC1 (green) and PIINC2 (red) with the previously published mutant structure (1QY7; blue). The structures are shown in two perspectives (top and side views), which are related to each other through a rotation around the x axis by 90°. The structures show significant deviations (yellow arrows) in the T-loop conformations and the C-terminal extensions (CT), which strongly depend on the crystallographic environment of the protein trimer. B, crystallographic packing of the PIINC1 structure, which shows that the C-terminal β-strand β6 is not formed due to crystallographic contacts (encircled by dotted lines) of trimers via their β5 strands.