2FSD

A Common Fold for the Receptor Binding Domains of Lactococcal Phages? The Crystal Structure of the Head Domain of Phage bIL170

Summary for 2FSD

• Entry DOI: 10.2210/pdb2fsd/pdb
• Descriptor: putative baseplate protein (2 entities in total)
• Functional Keywords: phage, lactococcus lactis, receptor binding protein, head domain, viral protein
• Biological source: unidentified phage
• Total number of polymer chains: 2
• Total formula weight: 30568.38

Authors

Ricagno, S.,Cambillau, C. (deposition date: 2006-01-22, release date: 2006-09-05, Last modification date: 2024-03-13)

Primary citation

Ricagno, S.,Campanacci, V.,Blangy, S.,Spinelli, S.,Tremblay, D.,Moineau, S.,Tegoni, M.,Cambillau, C.
Crystal Structure of the Receptor-Binding Protein Head Domain from Lactococcus lactis Phage bIL170
J.Virol., 80:9331-9335, 2006

PubMed Abstract: 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.

PubMed: 16940545
DOI: 10.1128/JVI.01160-06

Experimental method

X-RAY DIFFRACTION (2.3 Å)