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PDBsum entry 1g2h
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Transcription
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PDB id
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1g2h
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Contents |
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* Residue conservation analysis
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Protein Sci
10:592-598
(2001)
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PubMed id:
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Solution structure of the DNA-binding domain of the TyrR protein of Haemophilus influenzae.
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Y.Wang,
S.Zhao,
R.L.Somerville,
O.Jardetzky.
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ABSTRACT
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The TyrR protein of Haemophilus influenzae is a 36-kD transcription factor whose
major function is to control the expression of genes important in the
biosynthesis and transport of aromatic amino acids. Using (1)H and (15)N NMR
spectroscopy, we have determined the 3D solution structure of the TyrR
C-terminal DNA-binding domain (DBD) containing residues from 258 to 318
(TyrR[258-318]). The NMR results show that this segment of TyrR consists of a
potential hinge helix at its N terminus (residues 263-270) as well as three
well-defined alpha-helices extending from residues 277-289 (HR-2), 293-300
(HR-1), and 304-314 (HR). Helix HR-1 and HR fold in a typical helix-turn-helix
(HTH) motif. The three helices and the hinge helix are tightly bound together by
hydrophobic interaction and hydrogen bonds. Several hydrophilic residues whose
side chains may directly interact with DNA are identified. A hydrophobic patch
that may be part of the interaction surface between the domains of TyrR protein
is also observed. Comparisons with the structures of other HTH DNA-binding
proteins reveal that in terms of the spatial orientation of the three helices,
this protein most closely resembles the cap family.
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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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M.Musial-Siwek,
D.A.Kendall,
and
P.L.Yeagle
(2008).
Solution NMR of signal peptidase, a membrane protein.
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Biochim Biophys Acta,
1778,
937-944.
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T.Koyanagi,
T.Katayama,
H.Suzuki,
and
H.Kumagai
(2008).
Altered oligomerization properties of N316 mutants of Escherichia coli TyrR.
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J Bacteriol,
190,
8238-8243.
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J.Pittard,
H.Camakaris,
and
J.Yang
(2005).
The TyrR regulon.
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Mol Microbiol,
55,
16-26.
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L.Aravind,
V.Anantharaman,
S.Balaji,
M.M.Babu,
and
L.M.Iyer
(2005).
The many faces of the helix-turn-helix domain: transcription regulation and beyond.
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FEMS Microbiol Rev,
29,
231-262.
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P.Joseph,
M.Ratnayake-Lecamwasam,
and
A.L.Sonenshein
(2005).
A region of Bacillus subtilis CodY protein required for interaction with DNA.
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J Bacteriol,
187,
4127-4139.
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J.L.Huffman,
and
R.G.Brennan
(2002).
Prokaryotic transcription regulators: more than just the helix-turn-helix motif.
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Curr Opin Struct Biol,
12,
98.
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P.Ray,
K.J.Smith,
R.A.Parslow,
R.Dixon,
and
E.I.Hyde
(2002).
Secondary structure and DNA binding by the C-terminal domain of the transcriptional activator NifA from Klebsiella pneumoniae.
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Nucleic Acids Res,
30,
3972-3980.
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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.
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Links
