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Figure 2
Comparison between C. perfringens sortase D and representatives of classes A to D of transpeptidases. (a) The secondary structures of C. perfringens sortase D (CpSrtD; PDB entry 4d70 ), along with S. aureus sortase A (SaSrtA; PDB entry 1t2p ; Zong et al., 2004BB55), S. aureus sortase B (SaSrtB; PDB entry 1ng5 ; Zhang et al., 2004BB54), S. pneumoniae sortase C-2 (SpSrtC2; PDB entry 3g66 ; Neiers et al., 2009BB35) and B. anthracis sortase D (BaSrtC; PDB entry 2ln7 ; Robson et al., 2012BB39) are represented by red 310-helices and α-helices and yellow β-strands. The `lid' structure of the class C sortases is depicted in black, while the conserved cysteine, histidine and arginine residues are shown in purple, blue and orange, respectively. The conserved aspartate residue in SaSrtB is shown in pink. Figures were generated using PyMOL. (b) Sequence alignment between full-length CpSrtD, SaSrtA, SaSrtB, SpSrtC2 and BaSrtC, revealing identical amino acids (highlighted in red) and residues with high degree of similarity (highlighted in yellow). The conserved cysteine, histidine and arginine are indicated by asterisks. Sequence alignment was generated using ClustalW Omega (Goujon et al., 2010BB14; Sievers et al., 2011BB44).

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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