Structural highlights
FunctionFIB12_BPPH2 Structural component of the 12 appendages that hang from the lower collar. Adhesion protein that binds to the host cell surface during virus attachment and mediates teichoic acids degradation.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike.,Xiang Y, Leiman PG, Li L, Grimes S, Anderson DL, Rossmann MG Mol Cell. 2009 May 15;34(3):375-86. PMID:19450535[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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