Solution structure of the DNA-binding domain of the TyrR protein of Haemophilus influenzae

Protein Science : a Publication of the Protein Society
Y WangO Jardetzky

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.

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Citations

Apr 6, 2005·FEMS Microbiology Reviews·L AravindLakshminarayan M Iyer
Feb 13, 2002·Current Opinion in Structural Biology·Joy L Huffman, Richard G Brennan
Dec 23, 2004·Molecular Microbiology·James PittardJi Yang
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Dec 12, 2012·Nature Chemical Biology·Fa-An ChaoBurckhard Seelig
Jan 3, 2012·Journal of Structural Biology·Lakshminarayan M Iyer, L Aravind
Jan 8, 2008·Biochimica Et Biophysica Acta·Monika Musial-SiwekPhilip L Yeagle
Jul 7, 2016·Journal of Molecular Biology·Alistair James StandishRenato Morona
Feb 1, 2018·BMC Biotechnology·Yongfei LiuDawei Zhang

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