Solution Structure of Dimeric Mnt Repressor (1-76)

Burgering, Maurits; Boelens, Rolf; Gilbert, Dara E.; Breg, Jan; Knight, Kendall L.; Sauer, Robert T.; Kaptein, Robert

doi:10.1021/bi00254a012

Cited by 68 publications

(50 citation statements)

References 37 publications

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“…2A) similar to those previously determined for the transcriptional repressors Arc (53 residues) and Mnt (82 residues) of Salmonella enterica serovar Typhimurium bacteriophage P22 and 104-residue MetJ of Escherichia coli (3,4,20). All these proteins share a dimerizing 40-to 45-residue RHH motif (Fig.…”

Section: Features Of Copg and Comparison With Other Rhh Transcriptionsupporting

confidence: 84%

A Genetically Economical Family of Plasmid-Encoded Transcriptional Repressors Involved in Control of Plasmid Copy Number

et al. 2002

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Section: Features Of Copg and Comparison With Other Rhh Transcriptionsupporting

confidence: 84%

A Genetically Economical Family of Plasmid-Encoded Transcriptional Repressors Involved in Control of Plasmid Copy Number

et al. 2002

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“…This compact dimeric domain is characteristic of the RHH DNA-binding proteins (22), and its formation involves nearly every amino acid residue of ␤1, ␣1, and ␣2 of FitA (Fig. 3, a and b).…”

Section: Resultsmentioning

confidence: 99%

Structure of FitAB from Neisseria gonorrhoeae Bound to DNA Reveals a Tetramer of Toxin-Antitoxin Heterodimers Containing Pin Domains and Ribbon-Helix-Helix Motifs

Mattison

Wilbur

et al. 2006

Journal of Biological Chemistry

119

160

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Neisseria gonorrhoeae is a sexually transmitted pathogen that initiates infections in humans by adhering to the mucosal epithelium of the urogenital tract. The bacterium then enters the apical region of the cell and traffics across the cell to exit into the subepithelial matrix. Mutations in the fast intracellular trafficking (fitAB) locus cause the bacteria to transit a polarized epithelial monolayer more quickly than the wild-type parent and to replicate within cells at an accelerated rate. Here, we describe the crystal structure of the toxin-antitoxin heterodimer, FitAB, bound to a high affinity 36-bp DNA fragment from the fitAB promoter. FitA, the antitoxin, binds DNA through its ribbonhelix-helix motif and is tethered to FitB, the toxin, to form a heterodimer by the insertion of a four turn ␣-helix into an extensive FitB hydrophobic pocket. Neisseria gonorrhoeae (GC) 3 is the agent of the sexually transmitted disease, gonorrhea. The mechanisms used by GC to initiate infection have been very well characterized. Gonococci adhere via a multistep cascade and subsequently enter cells forming the epithelial barrier of the urogenital tract, traffic across these cells and exit into the subepithelial matrix (1, 2). Although studies have identified many of the molecular mechanisms used by GC to adhere to and enter cells, our knowledge of the mechanisms that operate in the later stages of infection is limited.GC are able to survive and grow within epithelial cells (3); they also traverse the epithelial monolayer to infect the stromal tissue of the subepithelium (2). The immune response to bacteria in the subepithelium produces the inflammation and purulent discharge characteristic of gonorrhea (4, 5). On occasion, GC establish a carrier state in which an asymptomatic individual harbors culturable and transmissible bacteria. These carriers are key to the spread of gonococcal disease, as humans are the only known reservoir for GC (6). The mechanisms by which GC maintains this persistent state are unknown. One hypothesis is that the organism resides within the epithelial cells instead of crossing into the subepithelium, thus evading the host immune response. The gene product(s) that affect GC intracellular growth and transcytosis are therefore important for the maintenance of gonococci in the human population.The fitAB operon was identified in a screen for GC mutants with a fast intracellular trafficking phenotype across polarized epithelial monolayers (3). A GC mutant that lacks fitAB grows normally extracellularly, but has an accelerated rate of intracellular replication with a concomitant increase in the rate at which this mutant traverses a monolayer of polarized epithelial cells. Thus, either FitA or FitB, or their complex, is hypothesized to slow intracellular replication and intracellular trafficking of GC.FitA is an 8.4-kDa protein with a predicted N-terminal ribbon-helix-helix (RHH) DNA binding motif (7,8). FitB is a 15.3-kDa protein with a predicted PIN (PilT-N terminus) domain according to the BLAST search t...

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“…The β-ribbon was formed by a typical alternating hydrophobic-hydrophilic pattern of amino acids (Leu%-Thr-Ile-Asp- [20,[31][32][33], it can be seen clearly that these residues are important for forming the hydrophobic core of this folding motif. The turn between the first and second helices starts in all cases with a glycine residue displaying the typical GXT\S pattern (Figure 4).…”

Section: Resonance Assignment and Structural Featuresmentioning

confidence: 99%

The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins

Oberer

Zangger

PRYTULLA³

et al. 2001

Biochemical Journal

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NMR and CD spectroscopy have been used to characterize, both structurally and dynamically, the 82-amino-acid ParD protein of the post-segregational killing module of the broad-host-range plasmid RP4\RK2. ParD occurs as a dimer in solution and exercises two different control functions ; an autoregulatory function by binding to its own promoter P parDE and a plasmidstabilizing function by inhibiting ParE toxicity in cells that express ParD and ParE. Analysis of the secondary structure based on the chemical-shift indices, sequential nuclear Overhauser enhancements (NOEs) and $J H α -NH scalar coupling constants showed that the N-terminal domain of ParD consists of a short β-ribbon followed by three α-helices, demonstrating that ParD contains a ribbon-helix-helix fold, a DNA-binding motif found in a family of small prokaryotic repressors. "&N longitudinal

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Solution Structure of Dimeric Mnt Repressor (1-76)

Cited by 68 publications

References 37 publications

A Genetically Economical Family of Plasmid-Encoded Transcriptional Repressors Involved in Control of Plasmid Copy Number

A Genetically Economical Family of Plasmid-Encoded Transcriptional Repressors Involved in Control of Plasmid Copy Number

Structure of FitAB from Neisseria gonorrhoeae Bound to DNA Reveals a Tetramer of Toxin-Antitoxin Heterodimers Containing Pin Domains and Ribbon-Helix-Helix Motifs

The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins

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