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PDBsum entry 3da0
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Viral protein
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PDB id
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3da0
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages.
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Authors
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M.Siponen,
S.Spinelli,
S.Blangy,
S.Moineau,
C.Cambillau,
V.Campanacci.
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Ref.
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J Bacteriol, 2009,
191,
3220-3225.
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PubMed id
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Abstract
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Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry
to manufacture cheeses, is subject to infection by a diverse population of
virulent phages. We have previously determined the structures of three receptor
binding proteins (RBPs) from lactococcal phages TP901-1, p2, and bIL170, each of
them having a distinct host range. Virulent phages p2 and bIL170 are classified
within the 936 group, while the temperate phage TP901-1 is a member of the
genetically distinct P335 polythetic group. These RBPs comprise three domains:
the N-terminal domain, binding to the virion particle; a beta-helical linker
domain; and the C-terminal domain, bearing the receptor binding site used for
host recognition. Here, we have designed, expressed, and determined the
structure of an RBP chimera in which the N-terminal and linker RBP domains of
phage TP901-1 (P335) are fused to the C-terminal RBP domain of phage p2 (936).
This chimera exhibits a stable structure that closely resembles the parental
structures, while a slight displacement of the linker made RBP domain adaptation
efficient. The receptor binding site is structurally indistinguishable from that
of native p2 RBP and binds glycerol with excellent affinity.
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