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TitleStructure of a VirD4 coupling protein bound to a VirB type IV secretion machinery.
Journal, issue, pagesEMBO J, Vol. 36, Issue 20, Page 3080-3095, Year 2017
Publish dateOct 16, 2017
AuthorsAdam Redzej / Marta Ukleja / Sarah Connery / Martina Trokter / Catarina Felisberto-Rodrigues / Adam Cryar / Konstantinos Thalassinos / Richard D Hayward / Elena V Orlova / Gabriel Waksman /
PubMed AbstractType IV secretion (T4S) systems are versatile bacterial secretion systems mediating transport of protein and/or DNA T4S systems are generally composed of 11 VirB proteins and 1 VirD protein (VirD4). ...Type IV secretion (T4S) systems are versatile bacterial secretion systems mediating transport of protein and/or DNA T4S systems are generally composed of 11 VirB proteins and 1 VirD protein (VirD4). The VirB1-11 proteins assemble to form a secretion machinery and a pilus while the VirD4 protein is responsible for substrate recruitment. The structure of VirD4 in isolation is known; however, its structure bound to the VirB1-11 apparatus has not been determined. Here, we purify a T4S system with VirD4 bound, define the biochemical requirements for complex formation and describe the protein-protein interaction network in which VirD4 is involved. We also solve the structure of this complex by negative stain electron microscopy, demonstrating that two copies of VirD4 dimers locate on both sides of the apparatus, in between the VirB4 ATPases. Given the central role of VirD4 in type IV secretion, our study provides mechanistic insights on a process that mediates the dangerous spread of antibiotic resistance genes among bacterial populations.
External linksEMBO J / PubMed:28923826 / PubMed Central
MethodsEM (single particle)
Resolution28.0 Å
Structure data

EMDB-3585:
Structure of the VirD4 bound to a Type IV secretion system
Method: EM (single particle) / Resolution: 28.0 Å

Source
  • Escherichia coli (E. coli)

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