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. 2010 Feb 1;107(9):4099–4104. doi: 10.1073/pnas.0911904107

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Fig. 4. — (A) Cartoon representation of PagP [PDB ID code 1THQ (19); W. L. DeLano, http://www.pymol.org (2002)] with Φ_F-values mapped onto the native structure. (B) Topology map of PagP highlighting the Φ_F-values of mutated residues. (C) Proposed folding mechanism of PagP into membranes: unfolded, but membrane-associated PagP (I); tilted insertion of the transition-state ensemble (II); and assembly of the helical clamp to yield native PagP (III). Note that the periplasmic halves of strands A, B, C, and D are depicted as loops to depict the low Φ_F-values of side-chains in this region of the transition-state structure. In A–C, Φ_F > 0.5 are in blue, 0.3 ≤ Φ_F ≤ 0.5 are in purple, Φ_F < 0.3 are in red, and Φ_F < 0 are in orange. Residues 51, 72, 108, 137, and 160 gave [the cut-off generally accepted to yield highly reliable Φ_F-values (41)].

Inline graphic — (A) Cartoon representation of PagP [PDB ID code 1THQ (19); W. L. DeLano, http://www.pymol.org (2002)] with Φ_F-values mapped onto the native structure. (B) Topology map of PagP highlighting the Φ_F-values of mutated residues. (C) Proposed folding mechanism of PagP into membranes: unfolded, but membrane-associated PagP (I); tilted insertion of the transition-state ensemble (II); and assembly of the helical clamp to yield native PagP (III). Note that the periplasmic halves of strands A, B, C, and D are depicted as loops to depict the low Φ_F-values of side-chains in this region of the transition-state structure. In A–C, Φ_F > 0.5 are in blue, 0.3 ≤ Φ_F ≤ 0.5 are in purple, Φ_F < 0.3 are in red, and Φ_F < 0 are in orange. Residues 51, 72, 108, 137, and 160 gave [the cut-off generally accepted to yield highly reliable Φ_F-values (41)].