Crystal structure of the receptor-binding protein head domain from Lactococcus lactis phage bIL170.
Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry, is subject to lytic phage infections. In the first step of infection, phages recognize the host saccharidic receptor using their receptor binding protein (RBP). Here, we report the 2.30-A-resolution crystal structure of the RBP head domain from phage bIL170. The structure of the head monomer is remarkably close to those of other lactococcal phages, p2 and TP901-1, despite any sequence identity with them. The knowledge of the three-dimensional structures of three RBPs gives a better insight into the module exchanges which have occurred among phages.
Ricagno
Stefano
S
Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités Aix-Marseille I & II, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
Campanacci
Valérie
V
Blangy
Stéphanie
S
Spinelli
Silvia
S
Tremblay
Denise
D
Moineau
Sylvain
S
Tegoni
Mariella
M
Cambillau
Christian
C
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000737:chemistry; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D007700:Kinetics; D013294:Lactococcus lactis / Q000821:virology*; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D004268:DNA-Binding Proteins