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-Structure paper
タイトル | High resolution CryoEM structure of the ring-shaped virulence factor EspB from . |
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ジャーナル・号・ページ | J Struct Biol X, Vol. 4, Page 100029, Year 2020 |
掲載日 | 2020年7月2日 |
著者 | Jérémie Piton / Florence Pojer / Soichi Wakatsuki / Cornelius Gati / Stewart T Cole / |
PubMed 要旨 | The EspB protein of is a 60 kDa virulence factor, implicated in conjugation and exported by the ESX-1 system of which it may also be a component. Previous attempts to obtain high-resolution maps of ...The EspB protein of is a 60 kDa virulence factor, implicated in conjugation and exported by the ESX-1 system of which it may also be a component. Previous attempts to obtain high-resolution maps of EspB by cryo-electron microscopic examination of single particles have been thwarted by severe orientation bias of the particles. This was overcome by using detergent as a surfactant thereby allowing reconstruction of the EspB structure at 3.37 Å resolution. The final structure revealed the N-terminal domain of EspB to be organized as a cylindrical heptamer with dimensions of 90 Å x 90 Å and a central channel of 45 Å diameter whereas the C-terminal domain was unstructured. New atomic insight was obtained into the helical packing required for protomer interactions and the overall electrostatic potential. The external surface is electronegatively charged while the channel is lined with electropositive patches. EspB thus has many features of a pore-like transport protein that might allow the passage of an ESX-1 substrate such as the 35 Å diameter EsxA-EsxB heterodimer or B-form DNA consistent with its proposed role in DNA uptake. |
リンク | J Struct Biol X / PubMed:32875288 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.37 Å |
構造データ | EMDB-10658, PDB-6xzc: |
由来 |
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キーワード | TRANSPORT PROTEIN / M. tuberculosis / ESX-1 / Type VII secretion system / EspB / Rv3881c / EsxA / CFP10 / ESAT-6 |