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

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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Somerville, R. L. Jardetzky, O. Wang, Y. Zhao, S.
Description	Country affiliation: United States Author Affiliation: Wang Y ( Department of Molecular Pharmacology, Stanford University, Stanford, CA 94305-5174, USA.)
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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	10
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2001-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Dna-binding Proteins Chemistry Escherichia Coli Proteins Haemophilus Influenzae Helix-turn-helix Motifs Repressor Proteins Molecular Conformation Protein Structure, Tertiary Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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