Matches in SemOpenAlex for { <https://semopenalex.org/work/W4220990596> ?p ?o ?g. }
- W4220990596 endingPage "167537" @default.
- W4220990596 startingPage "167537" @default.
- W4220990596 abstract "Portal proteins are dodecameric assemblies that occupy a unique 5-fold vertex of the icosahedral capsid of tailed bacteriophages and herpesviruses. The portal vertex interrupts the icosahedral symmetry, and in vivo, its assembly and incorporation in procapsid are controlled by the scaffolding protein. Ectopically expressed portal oligomers are polymorphic in solution, and portal rings built by a different number of subunits have been documented in the literature. In this paper, we describe the cryo-EM structure of the portal protein from the Pseudomonas-phage PaP3, which we determined at 3.4 Å resolution. Structural analysis revealed a dodecamer with helical rather than rotational symmetry, which we hypothesize is kinetically trapped. The helical assembly was stabilized by local mispairing of portal subunits caused by the slippage of crown and barrel helices that move like a lever with respect to the portal body. Removing the C-terminal barrel promoted assembly of undecameric and dodecameric rings with quasi-rotational symmetry, suggesting that the barrel contributes to subunits mispairing. However, ΔC-portal rings were intrinsically asymmetric, with most particles having one open portal subunit interface. Together, these data expand the structural repertoire of viral portal proteins to Pseudomonas-phages and shed light on the unexpected plasticity of the portal protein quaternary structure." @default.
- W4220990596 created "2022-04-03" @default.
- W4220990596 creator A5015918369 @default.
- W4220990596 creator A5040815738 @default.
- W4220990596 creator A5042025565 @default.
- W4220990596 creator A5045072018 @default.
- W4220990596 creator A5046791846 @default.
- W4220990596 creator A5059913267 @default.
- W4220990596 date "2022-05-01" @default.
- W4220990596 modified "2023-10-13" @default.
- W4220990596 title "Cryo-EM structure of a kinetically trapped dodecameric portal protein from the Pseudomonas-phage PaP3" @default.
- W4220990596 cites W1577039154 @default.
- W4220990596 cites W1955320271 @default.
- W4220990596 cites W1963803709 @default.
- W4220990596 cites W1965270719 @default.
- W4220990596 cites W1972966068 @default.
- W4220990596 cites W1975812347 @default.
- W4220990596 cites W1978802286 @default.
- W4220990596 cites W1983912680 @default.
- W4220990596 cites W1997824495 @default.
- W4220990596 cites W2004071147 @default.
- W4220990596 cites W2005323374 @default.
- W4220990596 cites W2012072946 @default.
- W4220990596 cites W2014957444 @default.
- W4220990596 cites W2015244557 @default.
- W4220990596 cites W2016196689 @default.
- W4220990596 cites W2027603822 @default.
- W4220990596 cites W2030517878 @default.
- W4220990596 cites W2033365137 @default.
- W4220990596 cites W2035503835 @default.
- W4220990596 cites W2046396780 @default.
- W4220990596 cites W2051762335 @default.
- W4220990596 cites W2057632446 @default.
- W4220990596 cites W2060788447 @default.
- W4220990596 cites W2063933749 @default.
- W4220990596 cites W2065364647 @default.
- W4220990596 cites W2068184659 @default.
- W4220990596 cites W2069309953 @default.
- W4220990596 cites W2073215770 @default.
- W4220990596 cites W2079273943 @default.
- W4220990596 cites W2080454444 @default.
- W4220990596 cites W2082423227 @default.
- W4220990596 cites W2098627436 @default.
- W4220990596 cites W2101889720 @default.
- W4220990596 cites W2104234755 @default.
- W4220990596 cites W2108342023 @default.
- W4220990596 cites W2121293808 @default.
- W4220990596 cites W2122339645 @default.
- W4220990596 cites W2124868860 @default.
- W4220990596 cites W2127332054 @default.
- W4220990596 cites W2132629607 @default.
- W4220990596 cites W2132740981 @default.
- W4220990596 cites W2144081223 @default.
- W4220990596 cites W2144998676 @default.
- W4220990596 cites W2152200928 @default.
- W4220990596 cites W2159244417 @default.
- W4220990596 cites W2161210875 @default.
- W4220990596 cites W2170141249 @default.
- W4220990596 cites W2515860409 @default.
- W4220990596 cites W2582282148 @default.
- W4220990596 cites W2583347981 @default.
- W4220990596 cites W2587625522 @default.
- W4220990596 cites W2593511418 @default.
- W4220990596 cites W2723380950 @default.
- W4220990596 cites W2734356283 @default.
- W4220990596 cites W2737241611 @default.
- W4220990596 cites W2763393774 @default.
- W4220990596 cites W2786390877 @default.
- W4220990596 cites W2788283510 @default.
- W4220990596 cites W2788833468 @default.
- W4220990596 cites W2794757315 @default.
- W4220990596 cites W2899714098 @default.
- W4220990596 cites W2912975498 @default.
- W4220990596 cites W2913226953 @default.
- W4220990596 cites W2914091207 @default.
- W4220990596 cites W2947914011 @default.
- W4220990596 cites W2953320394 @default.
- W4220990596 cites W2964062452 @default.
- W4220990596 cites W2969353230 @default.
- W4220990596 cites W2969732675 @default.
- W4220990596 cites W2970157772 @default.
- W4220990596 cites W2981168048 @default.
- W4220990596 cites W2982175283 @default.
- W4220990596 cites W3014243396 @default.
- W4220990596 cites W3016070378 @default.
- W4220990596 cites W3016178762 @default.
- W4220990596 cites W3029242200 @default.
- W4220990596 cites W3035719236 @default.
- W4220990596 cites W3043016901 @default.
- W4220990596 cites W3076562848 @default.
- W4220990596 cites W3096748979 @default.
- W4220990596 cites W3136158914 @default.
- W4220990596 cites W3159036185 @default.
- W4220990596 cites W3165127866 @default.
- W4220990596 cites W3173489521 @default.
- W4220990596 cites W3205562355 @default.
- W4220990596 cites W815604314 @default.
- W4220990596 doi "https://doi.org/10.1016/j.jmb.2022.167537" @default.