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-Structure paper
タイトル | A symmetry mismatch unraveled: How phage HK97 scaffold flexibly accommodates a 12-fold pore at a 5-fold viral capsid vertex. |
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ジャーナル・号・ページ | Sci Adv, Vol. 9, Issue 24, Page eadg8868, Year 2023 |
掲載日 | 2023年6月16日 |
著者 | Alexis Huet / Bonnie Oh / Josh Maurer / Robert L Duda / James F Conway / |
PubMed 要旨 | Tailed bacteriophages and herpesviruses use a transient scaffold to assemble icosahedral capsids with hexameric capsomers on the faces and pentameric capsomers at all but one vertex where a 12-fold ...Tailed bacteriophages and herpesviruses use a transient scaffold to assemble icosahedral capsids with hexameric capsomers on the faces and pentameric capsomers at all but one vertex where a 12-fold portal is thought to nucleate the assembly. How does the scaffold orchestrate this step? We have determined the portal vertex structure of the bacteriophage HK97 procapsid, where the scaffold is a domain of the major capsid protein. The scaffold forms rigid helix-turn-strand structures on the interior surfaces of all capsomers and is further stabilized around the portal, forming trimeric coiled-coil towers, two per surrounding capsomer. These 10 towers bind identically to 10 of 12 portal subunits, adopting a pseudo-12-fold organization that explains how the symmetry mismatch is managed at this early step. |
リンク | Sci Adv / PubMed:37327331 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.0 - 3.6 Å |
構造データ | EMDB-29389: HK97 portal, C12 symmetry EMDB-29390: Prohead I ico symmetry EMDB-29391: HK97 prohead I subsection -regular vertex. EMDB-29392: portal vertex of HK97 phage |
由来 |
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キーワード | VIRUS / Prohead I / icosahedral symmetry / HK97 / phage / capsid |