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-Structure paper
タイトル | Structure of the mycobacterial ESX-5 type VII secretion system pore complex. |
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ジャーナル・号・ページ | Sci Adv, Vol. 7, Issue 26, Year 2021 |
掲載日 | 2021年6月25日 |
著者 | Katherine S H Beckham / Christina Ritter / Grzegorz Chojnowski / Daniel S Ziemianowicz / Edukondalu Mullapudi / Mandy Rettel / Mikhail M Savitski / Simon A Mortensen / Jan Kosinski / Matthias Wilmanns / |
PubMed 要旨 | The ESX-5 type VII secretion system is a membrane-spanning protein complex key to the virulence of mycobacterial pathogens. However, the overall architecture of the fully assembled translocation ...The ESX-5 type VII secretion system is a membrane-spanning protein complex key to the virulence of mycobacterial pathogens. However, the overall architecture of the fully assembled translocation machinery and the composition of the central secretion pore have remained unknown. Here, we present the high-resolution structure of the 2.1-megadalton ESX-5 core complex. Our structure captured a dynamic, secretion-competent conformation of the pore within a well-defined transmembrane section, sandwiched between two flexible protein layers at the cytosolic entrance and the periplasmic exit. We propose that this flexibility endows the ESX-5 machinery with large conformational plasticity required to accommodate targeted protein secretion. Compared to known secretion systems, a highly dynamic state of the pore may represent a fundamental principle of bacterial secretion machineries. |
リンク | Sci Adv / PubMed:34172453 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.66 - 4.6 Å |
構造データ | EMDB-12103, PDB-7b9f: EMDB-12105, PDB-7b9s: EMDB-12674: PDB-7b7j: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | MEMBRANE PROTEIN / ubiqutin-like cytosolic ESX secretion / TRANSPORT PROTEIN / Mycobacterial ESX-5 Type VII Secretion System |