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6HN7

Hijacking the Hijackers: Escherichia coli Pathogenicity Islands Redirect Helper Phage Packaging for Their Own Benefit.

Summary for 6HN7
Entry DOI10.2210/pdb6hn7/pdb
DescriptorRedirecting phage packaging protein C (RppC), Terminase small subunit (3 entities in total)
Functional Keywordsredirecting packaging protein, dna binding protein, hetero-dimer, phage interference, protein complex
Biological sourceEscherichia coli
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Total number of polymer chains2
Total formula weight29301.11
Authors
Penades, J.R.,Bacarizo, J.,Marina, A.,Alqasmi, M.,Fillol-Salom, A.,Roszak, A.W.,Ciges-Tomas, J.R. (deposition date: 2018-09-14, release date: 2019-07-31, Last modification date: 2024-01-24)
Primary citationFillol-Salom, A.,Bacarizo, J.,Alqasmi, M.,Ciges-Tomas, J.R.,Martinez-Rubio, R.,Roszak, A.W.,Cogdell, R.J.,Chen, J.,Marina, A.,Penades, J.R.
Hijacking the Hijackers: Escherichia coli Pathogenicity Islands Redirect Helper Phage Packaging for Their Own Benefit.
Mol.Cell, 75:1020-1030.e4, 2019
Cited by
PubMed Abstract: Phage-inducible chromosomal islands (PICIs) represent a novel and universal class of mobile genetic elements, which have broad impact on bacterial virulence. In spite of their relevance, how the Gram-negative PICIs hijack the phage machinery for their own specific packaging and how they block phage reproduction remains to be determined. Using genetic and structural analyses, we solve the mystery here by showing that the Gram-negative PICIs encode a protein that simultaneously performs these processes. This protein, which we have named Rpp (for redirecting phage packaging), interacts with the phage terminase small subunit, forming a heterocomplex. This complex is unable to recognize the phage DNA, blocking phage packaging, but specifically binds to the PICI genome, promoting PICI packaging. Our studies reveal the mechanism of action that allows PICI dissemination in nature, introducing a new paradigm in the understanding of the biology of pathogenicity islands and therefore of bacterial pathogen evolution.
PubMed: 31350119
DOI: 10.1016/j.molcel.2019.06.017
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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