Skip to main content
. Author manuscript; available in PMC: 2010 Feb 24.
Published in final edited form as: Biochemistry. 2009 Feb 24;48(7):1532–1542. doi: 10.1021/bi801942a

Figure 1. The 2.0 Å structure of selenomethionine-substituted BT1043.

Figure 1

(A) Cartoon representation of the apo BT1043, colored blue to red from N- to C-terminus. The N-acetyl lactosamine ligand (magenta spheres) has been modeled in to show the location of the glycan-binding pocket. The 18 α-helices and 6 β-strands are labeled as shown; 310 helices are not labeled. Four helix-turn-helix pairs, or tetratrico peptide repeats (TPRs), are labeled with α1 & α4 as TPR1, α5 & α6 as TPR2, α7 & α8 as TPR3, and α12 & α13 as TPR4. (B) Overlay of BT1043, shown in blue, SusD (PDB 3CK7), shown in green, and BT3984 (PDB 3CGH) shown in red, in a similar view as in panel A to highlight to similarities in the TPR domain.