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. 2010 Sep 17;192(22):5953–5961. doi: 10.1128/JB.00417-10

FIG. 7.

FIG. 7.

Proposed model of Mep45 in the outer membrane. Shown are PRED-TMBB program predictions of transmembrane strands and the topology of Mep45. Transmembrane strands are shaded. The amino acid sequence with predicted high propensity to form an α-helical coiled-coil structure is underlined. Aromatic residues located near the ends of the transmembrane strand contacting the membrane surfaces are boxed. Proteinase K- and trypsin-sensitive cleavage sites are indicated as open and closed triangles, respectively.