 |
PDBsum entry 1g2h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
1g2h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Solution structure of the DNA-Binding domain of the tyrr protein of haemophilus influenzae.
|
|
|
Authors
|
|
Y.Wang,
S.Zhao,
R.L.Somerville,
O.Jardetzky.
|
|
|
Ref.
|
|
Protein Sci, 2001,
10,
592-598.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
