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PDBsum entry 1kaf
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Transcription
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PDB id
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1kaf
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PDB id:
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| Name: |
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Transcription
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Title:
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DNA binding domain of the phage t4 transcription factor mota (aa105- 211)
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Structure:
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Transcription regulatory protein mota. Chain: a, b, c, d, e, f. Fragment: DNA binding domain residues 105-211. Engineered: yes
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Source:
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Enterobacteria phage t4. Organism_taxid: 10665. Gene: mota. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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1.60Å
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R-factor:
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0.226
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R-free:
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0.258
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Authors:
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N.Li,E.A.Sickmier,R.Zhang,A.Joachimiak,S.W.White
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Key ref:
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N.Li
et al.
(2002).
The MotA transcription factor from bacteriophage T4 contains a novel DNA-binding domain: the 'double wing' motif.
Mol Microbiol,
43,
1079-1088.
PubMed id:
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Date:
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01-Nov-01
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Release date:
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21-Nov-01
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PROCHECK
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Headers
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References
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P22915
(MOTA_BPT4) -
Middle transcription regulatory protein motA from Enterobacteria phage T4
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Seq:
Struc:
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211 a.a.
108 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Mol Microbiol
43:1079-1088
(2002)
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PubMed id:
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The MotA transcription factor from bacteriophage T4 contains a novel DNA-binding domain: the 'double wing' motif.
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N.Li,
E.A.Sickmier,
R.Zhang,
A.Joachimiak,
S.W.White.
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ABSTRACT
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MotA is a transcription factor from bacteriophage T4 that helps adapt the host
Escherichia coli transcription apparatus to T4 middle promoters. We have
determined the crystal structure of the C-terminal DNA-binding domain of MotA
(MotCF) to 1.6 A resolution using multiwavelength, anomalous diffraction
methods. The structure reveals a novel DNA-binding alpha/beta motif that
contains an exposed beta-sheet surface that mediates interactions with the DNA.
Independent biochemical experiments have shown that MotCF binds to one surface
of a single turn of DNA through interactions in adjacent major and minor
grooves. We present a model of the interaction in which beta-ribbons at opposite
corners of the six-stranded beta-sheet penetrate the DNA grooves, and call the
motif a 'double wing' to emphasize similarities to the 'winged-helix' motif. The
model is consistent with data on how MotA functions at middle promoters, and
provides an explanation for why MotA can form non-specific multimers on DNA.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.M.Hinton
(2010).
Transcriptional control in the prereplicative phase of T4 development.
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Virol J,
7,
289.
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S.W.Nelson,
S.K.Perumal,
and
S.J.Benkovic
(2009).
Processive and unidirectional translocation of monomeric UvsW helicase on single-stranded DNA.
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Biochemistry,
48,
1036-1046.
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R.P.Bonocora,
G.Caignan,
C.Woodrell,
M.H.Werner,
and
D.M.Hinton
(2008).
A basic/hydrophobic cleft of the T4 activator MotA interacts with the C-terminus of E.coli sigma70 to activate middle gene transcription.
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Mol Microbiol,
69,
331-343.
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I.D.Kerr,
S.Sivakolundu,
Z.Li,
J.C.Buchsbaum,
L.A.Knox,
R.Kriwacki,
and
S.W.White
(2007).
Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4.
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J Biol Chem,
282,
34392-34400.
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PDB codes:
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K.K.Singarapu,
G.Liu,
R.Xiao,
C.Bertonati,
B.Honig,
G.T.Montelione,
and
T.Szyperski
(2007).
NMR structure of protein yjbR from Escherichia coli reveals 'double-wing' DNA binding motif.
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Proteins,
67,
501-504.
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PDB code:
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S.W.Nelson,
and
S.J.Benkovic
(2007).
The T4 phage UvsW protein contains both DNA unwinding and strand annealing activities.
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J Biol Chem,
282,
407-416.
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J.M.Nolan,
V.Petrov,
C.Bertrand,
H.M.Krisch,
and
J.D.Karam
(2006).
Genetic diversity among five T4-like bacteriophages.
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Virol J,
3,
30.
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E.A.Sickmier,
K.N.Kreuzer,
and
S.W.White
(2004).
The crystal structure of the UvsW helicase from bacteriophage T4.
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Structure,
12,
583-592.
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PDB code:
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M.Kamali-Moghaddam,
and
E.P.Geiduschek
(2003).
Thermoirreversible and thermoreversible promoter opening by two Escherichia coli RNA polymerase holoenzymes.
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J Biol Chem,
278,
29701-29709.
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S.Pande,
A.Makela,
S.L.Dove,
B.E.Nickels,
A.Hochschild,
and
D.M.Hinton
(2002).
The bacteriophage T4 transcription activator MotA interacts with the far-C-terminal region of the sigma70 subunit of Escherichia coli RNA polymerase.
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J Bacteriol,
184,
3957-3964.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
