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. 2017 Jun 1;13(6):e1006394. doi: 10.1371/journal.ppat.1006394

Fig 1. Crystal structures of SidK N-terminal domain.

Fig 1

Structures of SidK(16–278) were determined where one (A) and two (B) monomers were in the asymmetric unit. SidK(16–278) is an elongated protein comprised of three α-helical bundles ('Bundle I', 'Bundle II', 'Bundle III'). Bundle I includes two short α-helices that deviate from the main α-helical bundle axis (A, green arrowheads). C, In the crystal structure with two SidK monomers in the asymmetric unit, Bundle I is rotated ~180° with respect to Bundle II. This structural rearrangement allows the interface between Bundle I and Bundle II in the monomer structure (A, red oval and arrowhead) to be maintained in the dimer structure (B, red oval and arrowhead) through domain swapping between the two monomers. Scale bar: 25 Å.