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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Cryo-EM structure of the bacteria-killing type IV secretion system core complex from Xanthomonas citri

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Sgro, German G. [1, 2, 3] ; Costa, Tiago R. D. [2, 3, 4] ; Cenens, William [1] ; Souza, Diorge P. [1, 5] ; Cassago, Alexandre [6] ; de Oliveira, Luciana Coutinho [1, 7] ; Salinas, Roberto K. [1] ; Portugal, V, Rodrigo ; Farah, Chuck S. [1] ; Waksman, Gabriel [2, 3, 8]
Total Authors: 10
[1] Univ Sao Paulo, Inst Quim, Dept Bioquim, Sao Paulo - Brazil
[2] UCL, Inst Struct & Mol Biol, London - England
[3] Birkbeck Coll, Dept Biol Sci, London - England
[4] Imperial Coll London, Dept Life Sci, MRC Ctr Mol Bacteriol & Infect, London - England
[5] UCL, MRC Lab Mol Cell Biol, London - England
[6] V, CNPEM, Lab Nacl Nanotecnol LNNano, Campinas, SP - Brazil
[7] Univ Quebec, Dept Med Chem, INRS Inst Armand Frappier, Laval, PQ - Canada
[8] UCL, Div Biosci, Res Dept Struct & Mol Biol, Birkbeck Coll, London - England
Total Affiliations: 8
Document type: Journal article
Source: NATURE MICROBIOLOGY; v. 3, n. 12, p. 1429-1440, DEC 2018.
Web of Science Citations: 11

Type IV secretion (T4S) systems form the most common and versatile class of secretion systems in bacteria, capable of injecting both proteins and DNAs into host cells. T4S systems are typically composed of 12 components that form 2 major assemblies: the inner membrane complex embedded in the inner membrane and the core complex embedded in both the inner and outer membranes. Here we present the 3.3 angstrom-resolution cryo-electron microscopy model of the T4S system core complex from Xanthomonas citri, a phytopathogen that utilizes this system to kill bacterial competitors. An extensive mutational investigation was performed to probe the vast network of protein-protein interactions in this 1.13-MDa assembly. This structure expands our knowledge of the molecular details of T4S system organization, assembly and evolution. (AU)

FAPESP's process: 17/17303-7 - Structure and function of bacterial secretion systems
Grantee:Shaker Chuck Farah
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 11/07777-5 - Cyclic di-GMP signaling and the Type IV macromolecule secretion system in Xanthomonas citri
Grantee:Shaker Chuck Farah
Support Opportunities: Research Projects - Thematic Grants