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Figure 3 | BMC Microbiology

Figure 3

From: The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design

Figure 3

Superposition of alanine racemase monomers from Gram-positive bacteria. (A) Cα atom traces of alanine racemases from G. stearothermophilus (yellow) [29], E. faecalis (green) [38], B. anthracis (blue) [36], S. lavendulae (red) [33], and S. pneumoniae (pink). The superposed N-terminal α/β barrel domains are oriented on the bottom of the picture and the C-terminal β-strand domains on the top. Spheres represent the three structurally equivalent residues used to measure the hinge angle in each structure. The double-headed arrow indicates the variation between hinge angles. The PLP-bound Lys residue from AlrSP is shown in black. (B) Superposed ribbon representations of the N-terminal domains from E. faecalis (green) [38] and S. pneumoniae (pink), with the most divergent regions colored orange.

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