Three-dimensional solution structure of the N-terminal receiver domain of NTRC

Journal Article · Tue Jan 31 04:00:00 EST 1995 · Biochemistry (Eaton)

DOI:https://doi.org/10.1021/bi00004a036· OSTI ID:468994

Volkman, B F; Wemmer, D E; Nohaile, M J ^[1]

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1. Lawrence Berkeley Lab., CA (United States); and others

NTRC is a transcriptional enhancer binding protein whose N-terminal domain is a member of the family of receiver domains of two-component regulatory systems. Using 3D and 4D NMR spectroscopy, we have completed the {sup 1}H, {sup 15}N, and {sup 13}C assignments and determined the solution structure of the N-terminal receiver domain of the NTRC protein. Determination of the three-dimensional structure was carried out with the program X-PLOR using a total of 915 NMR-derived distance and dihedral angle restraints. The resultant family of structures has an average root mean square deviation of 0.81 {angstrom} from the average structure for the backbone atoms involved in well-defined secondary structure. The structure is comprised of five {alpha}-helices and f five-stranded parallel {beta}-sheet, in a ({beta}/{alpha}){sub 5} topology. Comparison of the solution structure of the NTRC receiver domain with the crystal structures of the homologous protein CheY in both the Mg{sup 2+}-free and Mg{sup 2+}-bound forms reveals a very similar fold, with the only significant difference occurring in the positioning of helix 4 relative to the rest of the protein. Examination of the conformation of consensus residues of the receiver domain superfamily in the structures of the NTRC receiver domain and CheY establishes the structural importance of residues whose side chains are involved in hydrogen bonding or hydrophobic core interactions. The importance of some nonconsensus residues which may be conserved for their ability to fulfill helix capping roles is also discussed. 67 refs., 9 figs., 1 tab.

• Sponsoring Organization: USDOE
• DOE Contract Number: AC03-76SF00098; FG05-86ER75281
• OSTI ID: 468994
• Journal Information: Biochemistry (Eaton), Journal Name: Biochemistry (Eaton) Journal Issue: 4 Vol. 34; ISSN 0006-2960; ISSN BICHAW
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
66 PHYSICS
CARBON 13
HYDROGEN 1
MOLECULAR STRUCTURE
NITROGEN 15
NMR SPECTRA
PHOSPHORYLATION
PROTEIN STRUCTURE
PROTEINS
RESIDUES
SALMONELLA TYPHIMURIUM
STRUCTURE-ACTIVITY RELATIONSHIPS