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PDBsum entry 3gq7
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Viral protein
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PDB id
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3gq7
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References listed in PDB file
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Key reference
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Title
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Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike.
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Authors
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Y.Xiang,
P.G.Leiman,
L.Li,
S.Grimes,
D.L.Anderson,
M.G.Rossmann.
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Ref.
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Mol Cell, 2009,
34,
375-386.
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PubMed id
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Abstract
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The tailed bacteriophage phi29 has 12 "appendages" (gene product 12, gp12)
attached to its neck region that participate in host cell recognition and entry.
In the cell, monomeric gp12 undergoes proteolytic processing that releases the
C-terminal domain during assembly into trimers. We report here crystal
structures of the protein before and after catalytic processing and show that
the C-terminal domain of gp12 is an "autochaperone" that aids trimerization. We
also show that autocleavage of the C-terminal domain is a posttrimerization
event that is followed by a unique ATP-dependent release. The
posttranslationally modified N-terminal part has three domains that function to
attach the appendages to the phage, digest the cell wall teichoic acids, and
bind irreversibly to the host, respectively. Structural and sequence comparisons
suggest that some eukaryotic and bacterial viruses as well as bacterial adhesins
might have a similar maturation mechanism as is performed by phi29 gp12 for
Bacillus subtilis.
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