8v8b
Structure of 80alpha portal protein expressed in E. coliStructure of 80alpha portal protein expressed in E. coli
Structural highlights
Publication Abstract from PubMedStaphylococcus aureus is an important human pathogen, and the prevalence of antibiotic resistance is a major public health concern. The evolution of pathogenicity and resistance in S. aureus often involves acquisition of mobile genetic elements (MGEs). Bacteriophages play an especially important role, since transduction represents the main mechanism for horizontal gene transfer. S. aureus pathogenicity islands (SaPIs), including SaPI1, are MGEs that carry genes encoding virulence factors, and are mobilized at high frequency through interactions with specific "helper" bacteriophages, such as 80alpha, leading to packaging of the SaPI genomes into virions made from structural proteins supplied by the helper. Among these structural proteins is the portal protein, which forms a ring-like portal at a fivefold vertex of the capsid, through which the DNA is packaged during virion assembly and ejected upon infection of the host. We have used high-resolution cryo-electron microscopy to determine structures of the S. aureus bacteriophage 80alpha portal itself, produced by overexpression, and in situ in the empty and full SaPI1 virions, and show how the portal interacts with the capsid. These structures provide a basis for understanding portal and capsid assembly and the conformational changes that occur upon DNA packaging and ejection. Structure of the Portal Complex from Staphylococcus aureus Pathogenicity Island 1 Transducing Particles In Situ and In Isolation.,Mukherjee A, Kizziah JL, Hawkins NC, Nasef MO, Parker LK, Dokland T J Mol Biol. 2023 Dec 21;436(4):168415. doi: 10.1016/j.jmb.2023.168415. PMID:38135177[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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