 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](tb5074fig1mag.jpg)
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Figure 1
(a) Overall structure of LmTBCA. The helices are represented as red ribbons. Ala43 and Pro80 are labelled as the approximate positions of bends in α1 and α2. A sulfate is bound to the surface of α1. (b) A closer view of the anion interacting with Arg45 and Arg49 is shown as gold (S) and red (O) sticks. The arginine residues are coloured by element (C, grey; N, blue) and two water molecules are depicted as red spheres. Blue mesh represents electron density (2mFo − DFc contoured at 2σ) and magenta dotted lines indicate potential hydrogen bonds. (c) The LmTBCA monomer (red) and a symmetry-related molecule (orange) are linked by a disulfide bond between Cys58 residues with side-chain atoms shown as sticks (C, grey; S, gold). The OMIT Fo − Fc density for the side-chain atoms of Cys58 and the symmetry mate is depicted as chickenwire and contoured at 2σ. (d) Backbone hydrogen bonds on α2. The expanded area is a stereoview of α1 and α3 as purple ribbons. α2 is depicted as pale pink ribbons (left) or as sticks coloured by element (right). Black dashed lines represent standard α-helical hydrogen bonds. Pro80 disrupts this bonding pattern. The magenta line between Pro80 N and Gln76 O represents a distance of 4.20 Å. |
![[Figure 1]](tb5074fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
