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. 2012 May 16;287(27):22910–22918. doi: 10.1074/jbc.M112.367128

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 1. — Overall structure of BgaC and its comparison with the other two GH-35 β-galactosidases. A, BgaC homodimer. The dimer is viewed along the noncrystallographic 2-fold axis. The three domains are colored in cyan, red, and yellow, respectively. The linker between the first and second domain is colored in blue. B, structural comparison with H. sapiens β-gal and Penicillium sp. β-gal. H. sapiens β-gal and Penicillium sp. β-gal are shown in the same view as BgaC. The corresponding domains are colored as those of BgaC, whereas the second domain and the third domain of Penicillium sp. β-gal are colored in green and orange, respectively.