File:Scau-china-2018-2.png

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BcsZ adopts an (α/α)6-barrel fold. BcsZ is shown as a cartoon from a top (A) and side (B) view. The inner and outer helices are shown in dark and pale green, respectively, and the three β-sheets flanking the substrate binding cleft are shown in blue. The catalytic residues Glu55 and Asp243 are shown as red sticks. Helices are labeled H1–H12 from the N to the C terminus. The C-terminal residues 349–357 of BcsZ form a two-stranded β-sheet (colored orange) on the opposite side of the substrate binding pocket.

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current10:07, 13 October 2018Thumbnail for version as of 10:07, 13 October 20181,028 × 445 (461 KB)Yinpin Huang (Talk | contribs)BcsZ adopts an (α/α)6-barrel fold. BcsZ is shown as a cartoon from a top (A) and side (B) view. The inner and outer helices are shown in dark and pale green, respectively, and the three β-sheets flanking the substrate binding cleft are shown in...
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