1g2h
From Proteopedia
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SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF THE TYRR PROTEIN OF HAEMOPHILUS INFLUENZAE
Overview
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.
About this Structure
1G2H is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Solution structure of the DNA-binding domain of the TyrR protein of Haemophilus influenzae., Wang Y, Zhao S, Somerville RL, Jardetzky O, Protein Sci. 2001 Mar;10(3):592-8. PMID:11344327
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