Figure 2
Three-dimensional structure of the BsrV dimer. (a) Crystal structure of a BsrV dimer with monomers depicted in yellow and blue. PLP molecules are shown in sticks and Cl− ions are shown as green spheres. (b) Structural superimposition of BsrV coloured as in (a) and Ala racemase from E. coli (AlrEc) in brown. Loops L1 and L2 and α-helix α10 at the entry channel are labelled [six residues in L1 (204–210) and 11 residues in L2 (267–278) in BstV versus ten residues in L1 (159–169) and 18 residues (216–234) in L2 in AlrEc]. On the right, differences in their active-site cavities are shown. White arrows show the dimensions of the entrance of the BsrV cavity. At the bottom of (b), a 180° rotation view (back side) of the dimer is shown and the BsrV N-terminal insertion is highlighted in the box (bottom right). The position of the N-terminal residue for both monomers in the AlrEc structure is marked by an asterisk. In the close-up view of the back-side region of BsrV, the N-terminal insertion is shown as sticks. Polar interactions between the N-terminal extensions from both monomers are represented as dotted lines. The position of Pro25 is indicated by a red arrow. (c) Different oligomeric arrangement between BsrV and AlrEc and its effect on the spatial distribution of the active sites. A schematic representation of the AlrEc and BsrV dimers is shown on the left; asterisks mark active sites. A rotation of 9° between monomers is produced by the N-terminal insertion in BsrV. Bottom left, structural superimposition of BsrV and AlrEc (brown cartoon). Displacement of the BsrV structural core by the N-terminal insertion (sticks) is represented by black arrows. Molecular surfaces for AlrEc and BsrV are shown on the right. The positions of active sites are marked by white circles and differences in distances and position of BsrV active sites versus Alr are highlighted. See also Supplementary Fig. S2. |