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Figure 2
The crystal structures of the discussed N-terminally truncated bacterial CdaAs are presented. (a) Superposition of S. pneumoniae (violet), B. subtilis (lime) and E. faecium (light blue) CdaA monomers reveals high structural similarity between the reported structures. A conserved tyrosine residue important for catalytic activity is depicted in stick representation. (b) Surface representation of the BsCdaA monomer colored by sequence-conservation score. The orientation corresponds to that in (a). Fragment molecules are depicted as sticks, and those bound to sequence-conserved areas are labeled. (c) Different orientations of the BsCdaA monomer depicted in (b).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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