15N relaxation data and model-free parameters for the N-terminal receiver domain
of double-mutant (D86N/A89T) unphosphorylated NtrC receiver domain
(NtrCr(D86N/A89T))

The molecule studied here contains two amino acid substitutions (D86N and A89T)
relative to the wild-type domain structure reported in this PDB entry.

Two-state allosteric behavior in a single domain signaling protein

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 1H, 15N, and 13C
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 (Brunger, 1992) 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 A from the average
structure for the backbone atoms involved in well-defined secondary structure.
The structure is comprised of five alpha-helices and a five-stranded parallel
beta-sheet, in a (beta/alpha)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(2+)-free and Mg(2+)-bound forms [Stock, A.M.,
Mottonen, J. M., Stock, J. B., & Schutt, C. E. (1989) Nature 337, 745-749;
Volz, K., & Matsumura, P. (1991) J. Biol. Chem. 296, 15511-15519; Stock, A. M.,
Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., &
Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J.,
Serrano, L., & Coll, M. (1994) J. Mol. Biol. 238, 489-495] 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 [Volz, K. (1993)
Biochemistry 32, 11741-11753] 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.

Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE.
Three-dimensional solution structure of the N-terminal receiver domain of NTRC.
Biochemistry. 1995 Jan 31;34(4):1413-24.

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

This corresponds to the N-terminal 124 residues of the full-length
NtrC(D86N/A89T) protein.
This is the N-terminal receiver domain from the double mutant NtrC(D86N/A89T),
a constitutively active form of the protein NtrC (i.e., has partial activity
even when unphosphorylated).

Nitrogen regulatory protein C N-terminal receiver domain

Structure Of A Transiently Phosphorylated "switch" In Bacterial Signal Transduction

Minimized Average Structure Of Beryllofluoride-Activated Ntrc Receiver Domain: Model Structure Incorporating Active Site Contac

Solution Structure And Backbone Dynamics Of Beryllofluoride- Activated Ntrc Receiver Domain

Solution Structure Of Beryllofluoride-Activated Ntrc Receiver Domain: Model Structures Incorporating Active Site Contacts

Solution Structure Of The N-Terminal Receiver Domain Of Ntrc

nitrogen regulation protein NR(I) [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]

two-component system, response regulator [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]

nitrogen regulatory protein C [Salmonella enterica subsp. enterica serovar Typhimurium]

Two-component system, response regulator [Salmonella enterica subsp. enterica serovar Typhi str. CT18]

Two-component system, response regulator [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]

Two-component system, response regulator [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]

two-component system, response regulator [Salmonella enterica subsp. enterica serovar Paratyphi A str. AKU_12601]

EBP family response regulator in two-component regulatory system with GlnL [Salmonella enterica subsp. enterica serovar Typhimu

two-component system, response regulator [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]

two-component system, response regulator [Salmonella enterica subsp. enterica serovar Paratyphi A str. ATCC 9150]

response regulator in two-component regulatory system with GlnL (EBP family) [Salmonella enterica subsp. enterica serovar Chole

hypothetical protein SPAB_04968 [Salmonella enterica subsp. enterica serovar Paratyphi B str. SPB7]

Two-component system, response regulator STY3876 [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)

two-component system response regulator [Salmonella enterica subsp. enterica serovar Typhi str. CT18]

nitrogen regulation protein NR(I) [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

nitrogen regulation protein NR(I) [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]

nitrogen regulation protein NR(I) [Salmonella enterica]

RecName: Full=Nitrogen regulation protein NR(I) [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Salmonella enterica subsp. enterica serovar Typhimurium

This BMRB deposition contains 15N relaxation
parameters and model-free analysis results
for 15N-labeled receiver domain of the double
mutant NtrC(D86N/A89T), a partially active but
unphosphorylated form of the protein NtrC from
S. typhimurium. This study was undertaken in
conjunction with similar experiments performed
on two related forms of this protein, the
inactive unphosphorylated wild type form,
NtrCr, and the fully active, phosphorylated
wild-type domain, P-NtrCr. The results obtained
on the other two forms are contained in separate
BMRB depositions.

All pulse schemes utilized gradients for sensitivity
enhancement and selective pulses for water flip-back (Farrow,
N.A. et al, Biochemistry (1994), 33, 5984-6003. Data for R1
and R2 measurements were acquired with 16 scans per FID, 220
complex 15N points and 512 complex 1H points. Heteronuclear NOE
measurements were acquired similarly, but with 24 scans per
FID. Spectral widths at 750 (600) MHz were 10000 (8012.82) Hz
in the 1H dimension and 2222.22 (1778.09) Hz in the 15N
dimension. T2 values were obtained with 8 different durations
of the delay T: 7.2, 14.4, 21.6, 28.8, 43.2, 57.6, 86.4, 115.2
ms. T1 values were obtained with T = 10, 20, 60, 120, 200, 400,
800 and 1400 ms. Duplicate spectra were recorded for T = 10 and
400 ms (T1) and T = 7.2 and 57.6 ms (T2) for estimation of peak
height uncertainties.
Pulse programs used for this study for Bruker Avance NMR
spectrometers are available at
http://www.nmrfam.wisc.edu/~volkman/pp/pulprog.html
Both spectrometers were equipped with three-axis gradients
and triple-resonance probeheads.

Relaxation data of NtrCr wt phosporylated

Provided by Prof. Arthur G. Palmer of Columbia University.
Palmer, A. G.,Rance, M. & Wright, P. E. (1991)
J. Am. Chem. Soc. 113, 4371-4380.
Mandel, A. M.,Akke, M. & Palmer, A. G. (1995)
J. Mol. Bio 246, 144-163.