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Yorodumi- PDB-7b9s: Structure of the mycobacterial ESX-5 Type VII Secretion System he... -
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-Basic information
Entry | Database: PDB / ID: 7b9s | ||||||
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Title | Structure of the mycobacterial ESX-5 Type VII Secretion System hexameric pore complex | ||||||
Components |
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Keywords | TRANSPORT PROTEIN / Mycobacterial ESX-5 Type VII Secretion System | ||||||
Function / homology | Function and homology information hydrolase activity / ATP hydrolysis activity / DNA binding / ATP binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Mycobacterium xenopi RIVM700367 (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||
Authors | Chojnowski, G. / Ritter, C. / Beckham, K.S.H. / Mullapudi, E. / Rettel, M. / Savitski, M.M. / Mortensen, S.A. / Ziemianowicz, D. / Kosinski, J. / Wilmanns, M. | ||||||
Citation | Journal: Sci Adv / Year: 2021 Title: Structure of the mycobacterial ESX-5 type VII secretion system pore complex. Authors: 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 / Abstract: 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. | ||||||
History |
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-Structure visualization
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Structure viewer | Molecule: MolmilJmol/JSmol |
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PDBx/mmCIF format | 7b9s.cif.gz | 1.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7b9s.ent.gz | 1.3 MB | Display | PDB format |
PDBx/mmJSON format | 7b9s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b9/7b9s ftp://data.pdbj.org/pub/pdb/validation_reports/b9/7b9s | HTTPS FTP |
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-Related structure data
Related structure data | 12105MC 7b7jC 7b9fC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
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Noncrystallographic symmetry (NCS) | NCS domain:
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