@article {389,
	title = {The solution structure and interactions of CheW from Thermotoga maritima},
	journal = {Nature Structural Biology},
	volume = {9},
	number = {2},
	year = {2002},
	note = {ISI Document Delivery No.: 516PHTimes Cited: 35Cited Reference Count: 34},
	month = {Feb},
	pages = {121-125},
	type = {Article},
	abstract = {Using protein from the hyperthermophile Thermotoga maritima, we have determined the solution structure of CheW, an essential component in the formation of the bacterial chemotaxis signaling complex. The overall fold is similar to the regulatory domain of the chemotaxis kinase CheA. In addition, interactions of CheW with CheA were monitored by nuclear magnetic resonance (NMR) techniques. The chemical shift perturbation data show the probable contacts that CheW makes with CheA. In combination with previous genetic data, the structure also suggests a possible binding site for the chemotaxis receptor. These results provide a structural basis for a model in which CheW acts as a molecular bridge between CheA and the cytoplasmic tails of the receptor.},
	keywords = {BACTERIAL CHEMOTAXIS, BINDING DOMAIN, C-13-LABELED PROTEINS, ESCHERICHIA-COLI, HISTIDINE KINASE, KINASE CHEA, NMR EXPERIMENTS, RESONANCE ASSIGNMENTS, SECONDARY STRUCTURE, SIGNAL-TRANSDUCTION},
	isbn = {1072-8368},
	url = {<Go to ISI>://000173562000015},
	author = {Griswold, I. J. and Zhou, H. J. and Matison, M. and Swanson, R. V. and McIntosh, L. P. and Simon, M. I. and Dahlquist, F. W.}
}
@article {3956,
	title = {High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, SpoOF: Implications for phosphorylation and molecular recognition},
	journal = {Biochemistry},
	volume = {36},
	number = {33},
	year = {1997},
	note = {ISI Document Delivery No.: XR735Times Cited: 45Cited Reference Count: 78},
	month = {Aug},
	pages = {10015-10025},
	type = {Article},
	abstract = {NMR has been employed for structural and dynamic studies of the bacterial response regulator, SpoOF. This 124-residue protein is an essential component of the sporulation phosphorelay signal transduction pathway in Bacillus subtilis. Three-dimensional H-1, N-15, and C-13 experiments have been used to obtain full side chain assignments and the 1511 distance, 121 dihedral angle, and 80 hydrogen bonding restraints required for generating a family of structures (14 restraints per residue). The structures give a well-defined (alpha/beta)(5) fold for residues 4-120 with average rms deviations of 0.59 Angstrom for backbone heavy atoms and 1.02 Angstrom for all heavy atoms. Analyses of backbone N-15 relaxation measurements demonstrate relative rigidity in most regions of regular secondary structure with a generalized order parameter (S-2) Of 0.9 +/- 0.05 and a rotational correlation time (tau(m)) of 7.0 +/- 0.5 ns, Loop regions near the site of phosphorylation have higher than average rms deviation values and T-1/T-2 ratios suggesting significant internal motion or chemical exchange at these sites, Additionally, multiple conformers are observed for the beta 4-alpha 4 loop and beta-strand 5 region, These conformers may be related to structural changes associated with phosphorylation and also indicative of the propensity this recognition surface has for differential protein interactions. Comparison of SpoOF structural features to those of other response regulators reveals subtle differences in the orientations of secondary structure in the putative recognition surfaces and the relative charge distribution of residues surrounding the site of phosphorylation, These may be important in providing specificity for protein-protein interactions and for determining the lifetimes of the phosphorylated state.},
	keywords = {3-DIMENSIONAL STRUCTURE, BACTERIAL CHEMOTAXIS, C-13 MAGNETIZATION, C-13-ENRICHED PROTEINS, C-13-LABELED PROTEINS, ESCHERICHIA-COLI, MAGNESIUM-BINDING, NUCLEAR-MAGNETIC-RESONANCE, PROTEIN SECONDARY STRUCTURE, SIGNAL-TRANSDUCTION},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1997XR73500007},
	author = {Feher, V. A. and Zapf, J. W. and Hoch, J. A. and Whiteley, J. M. and McIntosh, L. P. and Rance, M. and Skelton, N. J. and Dahlquist, F. W. and Cavanah, J.}
}
