Crystallographic Insights into the Autocatalytic Assembly Mechanism of a Bacteriophage Tail Spike

Ye Xiang, Petr G. Leiman, Long Li, Shelley Grimes, Dwight L. Anderson, Michael G. Rossmann

Research output: Contribution to journalArticlepeer-review

65 Scopus citations


The tailed bacteriophage φ{symbol}29 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 φ{symbol}29 gp12 for Bacillus subtilis.

Original languageEnglish (US)
Pages (from-to)375-386
Number of pages12
JournalMolecular Cell
Issue number3
StatePublished - May 15 2009

Bibliographical note

Funding Information:
We thank James L. VanEtten for providing the corrected PBCV Vp260 sequence and Wallace Muhonen for preparing the gp12 ∗ appendages from mutant phage-infected cells. We are grateful to Sheryl Kelly and Carol Greski for help in preparing the manuscript. We thank the staff at Argonne National Laboratory's Advanced Photon Source (BioCARS, SER-CAT, and GM/CA-CAT sectors) for their help. These facilities are supported by the U.S. Department of Energy and/or the National Institutes of Health (NIH). This work was supported by a National Science Foundation grant (MCB-0443899) to M.G.R. and a NIH grant (DE003606) to D.L.A., S.G., and M.G.R.




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