2L8T

Staphylococcus aureus pathogenicity island 1 protein gp6, an internal scaffold in size determination

Summary for 2L8T

• Entry DOI: 10.2210/pdb2l8t/pdb
• NMR Information: BMRB: 17425
• Descriptor: Transposon Tn557 toxic shock syndrome toxin-1 (1 entity in total)
• Functional Keywords: scaffold, bacteriophage, sapi, structural protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 16300.08

Authors

Dearborn, A.D.,Spilman, M.S.,Damle, P.K.,Chang, J.R.,Monroe, E.B.,Saad, J.S.,Christie, G.E.,Dokland, T. (deposition date: 2011-01-24, release date: 2011-08-17, Last modification date: 2024-05-01)

Primary citation

Dearborn, A.D.,Spilman, M.S.,Damle, P.K.,Chang, J.R.,Monroe, E.B.,Saad, J.S.,Christie, G.E.,Dokland, T.
The Staphylococcus aureus Pathogenicity Island 1 Protein gp6 Functions as an Internal Scaffold during Capsid Size Determination.
J.Mol.Biol., 412:710-722, 2011

PubMed Abstract: Staphylococcus aureus pathogenicity island 1 (SaPI1) is a mobile genetic element that carries genes for several superantigen toxins. SaPI1 is normally stably integrated into the host genome but can become mobilized by "helper" bacteriophage 80α, leading to the packaging of SaPI1 genomes into phage-like transducing particles that are composed of structural proteins supplied by the helper phage but having smaller capsids. We show that the SaPI1-encoded protein gp6 is necessary for efficient formation of small capsids. The NMR structure of gp6 reveals a dimeric protein with a helix-loop-helix motif similar to that of bacteriophage scaffolding proteins. The gp6 dimer matches internal densities that bridge capsid subunits in cryo-electron microscopy reconstructions of SaPI1 procapsids, suggesting that gp6 acts as an internal scaffolding protein in capsid size determination.

PubMed: 21821042
DOI: 10.1016/j.jmb.2011.07.036

Experimental method

SOLUTION NMR