Structure of the double-stranded DNA-binding type IV secretion protein TraN from Enterococcus

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 70; no. 9; pp. 2376 - 2389
• Main Authors: Goessweiner-Mohr, Nikolaus, Eder, Markus, Hofer, Gerhard, Fercher, Christian, Arends, Karsten, Birner-Gruenberger, Ruth, Grohmann, Elisabeth, Keller, Walter
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.09.2014; Wiley Subscription Services, Inc
• Subjects: Accessories; Antiinfectives and antibacterials; Bacteria; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Base Sequence; Binding Sites; Crystallography, X-Ray; DNA binding; DNA Primers; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - metabolism; Enterococcus; Enterococcus faecalis; Enterococcus faecalis - chemistry; Enterococcus faecium; Enterococcus faecium - chemistry; Gram positive; internal dimer; Mass Spectrometry; Protein Conformation; Proteins; Regulators; Secretions; Spreading; Subcellular Fractions - metabolism; type IV secretion; Upstream; Enterococcus; internal dimer; type IV secretion; Gram positive; DNA binding

Conjugative transfer through type IV secretion multiprotein complexes is the most important means of spreading antimicrobial resistance. Plasmid pIP501, frequently found in clinical Enterococcus faecalis and Enterococcus faecium isolates, is the first Gram‐positive (G+) conjugative plasmid for which...