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Figure 2 | BMC Biology

Figure 2

From: The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae

Figure 2

The N-terminus of Par17 includes an amphipatic α-helix. A. Secondary structure of Par17. The N-terminal Par17 sequence from Met3 to Ala23 is predicted to adopt α-helical conformation ("H") by different algorithms within the NPS prediction package, whereas the remaining part of this sequence is predicted to be random coil ("."). The PPIase domain starts at Asn61 with an extented beta-sheet ("e"). Consensus sequence prediction is based on HNNC, MLRC, PHD and Predator predictions. B. The N-terminal α-helix is amphipatic. Par17 protein sequence from Met3 to Ala23 is depicted as helical wheel with large, hydrophobic residues highlighted in grey, basic residues in blue and acidic ones in red.

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