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PMID:19861547

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Citation

Pang, T, Savva, CG, Fleming, KG, Struck, DK and Young, R (2009) Structure of the lethal phage pinhole. Proc. Natl. Acad. Sci. U.S.A. 106:18966-71

Abstract

Perhaps the simplest of biological timing systems, bacteriophage holins accumulate during the phage morphogenesis period and then trigger to permeabilize the cytoplasmic membrane with lethal holes; thus, terminating the infection cycle. Canonical holins form very large holes that allow nonspecific release of fully-folded proteins, but a recently discovered class of holins, the pinholins, make much smaller holes, or pinholes, that serve only to depolarize the membrane. Here, we interrogate the structure of the prototype pinholin by negative-stain transmission electron-microscopy, cysteine-accessibility, and chemical cross-linking, as well as by computational approaches. Together, the results suggest that the pinholin forms symmetric heptameric structures with the hydrophilic surface of one transmembrane domain lining the surface of a central channel approximately 15 A in diameter. The structural model also suggests a rationale for the prehole state of the pinholin, the persistence of which defines the duration of the viral latent period, and for the sensitivity of the holin timing system to the energized state of the membrane.

Links

PubMed PMC2776468 Online version:10.1073/pnas.0907941106

Keywords

Amino Acid Sequence; Bacteriolysis/physiology; Bacteriophages/chemistry; Chromatography, Gel; Microscopy, Electron, Transmission; Models, Molecular; Molecular Sequence Data; Protein Conformation; Viral Proteins/ultrastructure

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

BPP21:VLYS

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P27360

F

Seeded From UniProt

complete

BPP21:HOLIN

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P27360

F

Seeded From UniProt

complete

Notes

See also

References

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