Crystal structure of apo-ClfB_(197–542).

Abstract

<p>A. Domain organization of ClfB. The numbers of the amino acid residues identifying the boundaries between adjacent domains are indicated below. S, signal sequence; N1-3, N-terminal fibrinogen binding region; R, serine-aspartate repeat region; W, wall-spanning domain; M, membrane anchor; C, cytoplasmic positively charged tail. The N2 and N3 domains were used in crystallization of the ClfB_(197–542)-peptide complexes. B. Ribbon representation of the structure of apo-ClfB_(197–542), with its N and C terminus indicated. The N2 and N3 domains are shown in orange and magenta, respectively. The strands and loops are marked. C. Ribbon representation of the two symmetry-related molecules in the unit cell, shown in orange and magenta, respectively. The N and C termini of both molecules are indicated. D. Closer view of the interaction between the two symmetry-related molecules. The N-terminus of one molecule (amino acids 196–201) is shown as sticks and the other one is colored in magenta as in (B). The amino acids from both molecules are marked in red and black characters, respectively. The hydrogen bonds are shown as red dashed lines.</p