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Article

Protonation-mediated structural flexibility in the F conjugation regulatory protein, TraM.

The EMBO journal - 21 Jun 2006

Lu Jun, Edwards Ross A, Wong Joyce J W, Manchak Jan, Scott Paul G, Frost Laura S, Glover J N Mark

Abstract excerpt

TraM is essential for F plasmid-mediated bacterial conjugation, where it binds to the plasmid DNA near the origin of transfer, and recognizes a component of the transmembrane DNA transfer complex, TraD. Here we report the 1.40 A crystal structure of the TraM core tetramer (TraM58-127). TraM58-127 is a compact eight-helical bundle, in which the N-terminal helices from each protomer interact to form a central,...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 16710295
DOI: 10.1038/sj.emboj.7601151
PMCID: PMC1500842

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Protonation-mediated structural flexibility in the F conjugation regulatory protein, TraM.PMID 16710295Read ↗

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A rapid screen for functional mutants of TraM, an autoregulatory protein required for F conjugation.Semantic proximity Read ↗

Specific DNA recognition by F Factor TraY involves beta-sheet residues.Semantic proximity Read ↗

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