The ClfB-ligand binding is consistent with the DLL model.

Abstract

<p>A. Ribbon representation of the superimposition of apo-ClfB, ClfB-Fg α and ClfB-CK10 complexes. The apo-ClfB is shown in limon. In the ClfB-Fg α complex, the protein and Fg α are shown in magenta and marine, respectively. In the ClfB-CK10 complex, ClfB and CK10 are shown in orange and yellow, respectively. B. Closer view of the interactions between the C-terminal G′ strand of N3 domain and N2 domain in the ClfB-Fg α complex. Residues involved in the interactions from both G′ strand and N2 domain are shown as sticks and marked by blue and black characters, respectively. The Fg α peptide is shown as sticks in yellow. C. Structural alignment of the ClfB-Fg α complex solved in this study and the one by V.Ganesh et al. (PDB entry: 3AT0) shown in stereo view, with RMSD 0.635 Å. The ClfB-Fg α complex in this study is shown in orange and the peptide is shown as sticks in the same color. The ClfB in the corresponding structure by V.Ganesh et al. is shown in cyan and Fg α is shown as sticks with its N and C termini marked. The C termini of ClfB in both structures and the G′ strand of ClfB in the current study are indicated. D. Structural alignment of the ClfB-CK10 complex solved in this study and the one by V.Ganesh et al. (PDB entry: 3ASW), with RMSD 0.479 Å. The ClfB-CK10 complex in this study is shown in marine and the peptide is shown as sticks with its N and C termini marked. The ClfB in the corresponding structure by V.Ganesh et al. is shown in lime and CK10 is shown as sticks. The C-termini of ClfB in both structures are indicated.</p