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PDBsum entry 6chv
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Antitoxin/DNA
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PDB id
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6chv
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PDB id:
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| Name: |
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Antitoxin/DNA
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Title:
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Proteus vulgaris higa antitoxin bound to DNA
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Structure:
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Antitoxin higa. Chain: a, c, b, d, g, h. Synonym: antidote protein,host inhibition of growth protein a. Engineered: yes. Phigcryst3. Chain: i, e, k. Engineered: yes. Phigcryst4. Chain: j, f, l.
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Source:
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Proteus vulgaris. Organism_taxid: 585. Gene: higa. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 585
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Resolution:
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2.90Å
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R-factor:
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0.227
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R-free:
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0.260
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Authors:
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M.A.Schureck,E.D.Hoffer,N.Onuoha,C.M.Dunham
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Key ref:
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M.A.Schureck
et al.
(2019).
Structural basis of transcriptional regulation by the HigA antitoxin.
Mol Microbiol,
111,
1449-1462.
PubMed id:
DOI:
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Date:
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23-Feb-18
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Release date:
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27-Feb-19
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PROCHECK
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Headers
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References
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Q7A224
(HIGA_PROVU) -
Antitoxin HigA from Proteus vulgaris
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Seq:
Struc:
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104 a.a.
89 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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G-T-A-T-T-A-C-A-C-A-C-C-A-T-G-T-A-A-T-A-C
21 bases
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G-T-A-T-T-A-C-A-T-G-G-T-G-T-G-T-A-A-T-A-C
21 bases
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G-T-A-T-T-A-C-A-C-A-C-C-A-T-G-T-A-A-T-A-C
21 bases
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G-T-A-T-T-A-C-A-T-G-G-T-G-T-G-T-A-A-T-A-C
21 bases
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G-T-A-T-T-A-C-A-C-A-C-C-A-T-G-T-A-A-T-A-C
21 bases
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G-T-A-T-T-A-C-A-T-G-G-T-G-T-G-T-A-A-T-A-C
21 bases
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DOI no:
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Mol Microbiol
111:1449-1462
(2019)
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PubMed id:
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Structural basis of transcriptional regulation by the HigA antitoxin.
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M.A.Schureck,
J.Meisner,
E.D.Hoffer,
D.Wang,
N.Onuoha,
S.Ei Cho,
P.Lollar,
C.M.Dunham.
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ABSTRACT
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Bacterial toxin-antitoxin systems are important factors implicated in growth
inhibition and plasmid maintenance. Type II toxin-antitoxin pairs are regulated
at the transcriptional level by the antitoxin itself. Here, we examined how the
HigA antitoxin regulates the expression of the Proteus vulgaris higBA
toxin-antitoxin operon from the Rts1 plasmid. The HigBA complex adopts a unique
architecture suggesting differences in its regulation as compared to classical
type II toxin-antitoxin systems. We find that the C-terminus of the HigA
antitoxin is required for dimerization and transcriptional repression. Further,
the HigA structure reveals that the C terminus is ordered and does not
transition between disorder-to-order states upon toxin binding. HigA residue
Arg40 recognizes a TpG dinucleotide in higO2, an evolutionary conserved mode of
recognition among prokaryotic and eukaryotic transcription factors. Comparison
of the HigBA and HigA-higO2 structures reveals the distance between
helix-turn-helix motifs of each HigA monomer increases by ~4 Å in order to
bind to higO2. Consistent with these data, HigBA binding to each operator is
twofold less tight than HigA alone. Together, these data show the HigB toxin
does not act as a co-repressor suggesting potential novel regulation in this
toxin-antitoxin system.
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