Figure 2: Structural analysis of MapZextra. | Nature Communications

Figure 2: Structural analysis of MapZextra.

From: Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ

Figure 2

(a) Cartoon representation of the NMR ensemble of the 20 lowest-energy structures of MapZextra1 (lower structure) and MapZextra2 (upper structure). The ensemble on the right is rotated by 180° along the y axis compared with the structures on the left. The serine-rich linker (SRL) is pictured as a grey curved line. N- and C-terminal residues as well as α-helices are annotated. (b) Topology of the MapZextra2 subdomain. α-Helices and β-strands are represented by grey circles and arrows, respectively. (c) Topology of the MapZextra1 subdomain. Similarly to b, α-helices are shown as grey circles. The most significant residues that are implicated in hydrophobic interactions and maintain the global structure are displayed as white circles, while hydrophobic contacts are emphasized as dotted lines. In b and c, residues delimiting the loops pictured as black lines are indicated.

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