The Linker between the Dimerization and Catalytic Domains of the CheA Histidine Kinase Propagates Changes in Structure and Dynamics That Are Important for Enzymatic Activity
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L. Kay | F. Dahlquist | Chun Wu | Xiqing Wang | Anh Vu | J. Shea | Kwangwoon Lee | Wen‐Ju Bai | P. Vallurupalli | Sheng Sun | Hongjun Zhou
[1] J. S. Parkinson,et al. Mutational Analysis of the P1 Phosphorylation Domain in Escherichia coli CheA, the Signaling Kinase for Chemotaxis , 2013, Journal of bacteriology.
[2] Igor B. Zhulin,et al. The 3.2 Å resolution structure of a receptor: CheA:CheW signaling complex defines overlapping binding sites and key residue interactions within bacterial chemosensory arrays. , 2013, Biochemistry.
[3] Kene N. Piasta,et al. Defining a key receptor-CheA kinase contact and elucidating its function in the membrane-bound bacterial chemosensory array: a disulfide mapping and TAM-IDS Study. , 2013, Biochemistry.
[4] Joan-Emma Shea,et al. Computational and experimental analyses reveal the essential roles of interdomain linkers in the biological function of chemotaxis histidine kinase CheA. , 2012, Journal of the American Chemical Society.
[5] F. Dahlquist,et al. CheA-receptor interaction sites in bacterial chemotaxis. , 2012, Journal of molecular biology.
[6] Jun Liu,et al. Molecular architecture of chemoreceptor arrays revealed by cryoelectron tomography of Escherichia coli minicells , 2012, Proceedings of the National Academy of Sciences.
[7] G. Jensen,et al. Bacterial chemoreceptor arrays are hexagonally packed trimers of receptor dimers networked by rings of kinase and coupling proteins , 2012, Proceedings of the National Academy of Sciences.
[8] Hongjun Zhou,et al. The receptor-CheW binding interface in bacterial chemotaxis. , 2012, Journal of molecular biology.
[9] K. Ottemann,et al. Motility and chemotaxis in Campylobacter and Helicobacter . , 2011, Annual review of microbiology.
[10] María-Eugenia Guazzaroni,et al. Bacterial sensor kinases: diversity in the recognition of environmental signals. , 2010, Annual review of microbiology.
[11] J. Freed,et al. Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy. , 2010, Biochemistry.
[12] M. Kurosu,et al. Bacterial protein kinase inhibitors , 2010 .
[13] J. Falke,et al. Engineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor. , 2009, Biochemistry.
[14] J. S. Parkinson,et al. Mutational analyses of HAMP helices suggest a dynamic bundle model of input–output signalling in chemoreceptors , 2009, Molecular microbiology.
[15] S. Gloor,et al. Thermal domain motions of CheA kinase in solution: Disulfide trapping reveals the motional constraints leading to trans-autophosphorylation. , 2009, Biochemistry.
[16] Pramodh Vallurupalli,et al. Measurement of bond vector orientations in invisible excited states of proteins , 2007, Proceedings of the National Academy of Sciences.
[17] F. Dahlquist,et al. Chemical-shift-perturbation mapping of the phosphotransfer and catalytic domain interaction in the histidine autokinase CheA from Thermotoga maritima. , 2006, Biochemistry.
[18] J. Falke,et al. CheA Kinase of bacterial chemotaxis: chemical mapping of four essential docking sites. , 2006, Biochemistry.
[19] J. S. Parkinson,et al. Cysteine-Scanning Analysis of the Chemoreceptor-Coupling Domain of the Escherichia coli Chemotaxis Signaling Kinase CheA , 2006, Journal of bacteriology.
[20] Susan M. Butler,et al. Going against the grain: chemotaxis and infection in Vibrio cholerae , 2005, Nature Reviews Microbiology.
[21] Jian Zhang,et al. Dynamic mechanism for the autophosphorylation of CheA histidine kinase: molecular dynamics simulations. , 2005, Journal of the American Chemical Society.
[22] D. DeRosier,et al. Three-dimensional structure and organization of a receptor/signaling complex. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[23] G. Wadhams,et al. Making sense of it all: bacterial chemotaxis , 2004, Nature Reviews Molecular Cell Biology.
[24] W. Shi,et al. Chemotaxis-guided movements in bacteria. , 2004, Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists.
[25] L. Kay,et al. Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. , 2001, Journal of the American Chemical Society.
[26] A. Palmer,et al. A TROSY CPMG sequence for characterizing chemical exchange in large proteins , 1999, Journal of biomolecular NMR.
[27] Sung-Hou Kim,et al. Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor , 1999, Nature.
[28] A. Palmer,et al. A Relaxation-Compensated Carr−Purcell−Meiboom−Gill Sequence for Characterizing Chemical Exchange by NMR Spectroscopy , 1999 .
[29] Kurt Wüthrich,et al. TROSY-TYPE TRIPLE-RESONANCE EXPERIMENTS FOR SEQUENTIAL NMR ASSIGNMENTS OF LARGE PROTEINS , 1999 .
[30] M. Simon,et al. Structure of CheA, a Signal-Transducing Histidine Kinase , 1999, Cell.
[31] K Wüthrich,et al. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[32] D. Torchia,et al. Using Amide 1H and 15N Transverse Relaxation To Detect Millisecond Time-Scale Motions in Perdeuterated Proteins: Application to HIV-1 Protease , 1998 .
[33] R. Stewart,et al. TNP-ATP and TNP-ADP as probes of the nucleotide binding site of CheA, the histidine protein kinase in the chemotaxis signal transduction pathway of Escherichia coli. , 1998, Biochemistry.
[34] J. Hoch,et al. Two-Component Signal Transduction as a Target for Microbial Anti-Infective Therapy , 1998, Antimicrobial Agents and Chemotherapy.
[35] R. Riek,et al. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[36] J. S. Parkinson,et al. Chemotactic signaling by the P1 phosphorylation domain liberated from the CheA histidine kinase of Escherichia coli , 1996, Journal of bacteriology.
[37] M. Simon,et al. Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima , 1996, Journal of bacteriology.
[38] S. Grzesiek,et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.
[39] F. Dahlquist,et al. Signal transduction in chemotaxis. A propagating conformation change upon phosphorylation of CheY. , 1994, The Journal of biological chemistry.
[40] J. S. Parkinson,et al. Constitutively signaling fragments of Tsr, the Escherichia coli serine chemoreceptor , 1994, Journal of bacteriology.
[41] R. Bourret,et al. Intermolecular complementation of the kinase activity of CheA , 1993, Molecular microbiology.
[42] M. Simon,et al. The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW , 1993, Journal of bacteriology.
[43] Frederick W. Dahlquist,et al. Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway , 1992, Cell.
[44] J. Stock,et al. Reconstitution of the bacterial chemotaxis signal transduction system from purified components. , 1991, The Journal of biological chemistry.
[45] F. Dahlquist,et al. Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[46] M. Simon,et al. Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[47] J. Stock,et al. CheA protein, a central regulator of bacterial chemotaxis, belongs to a family of proteins that control gene expression in response to changing environmental conditions. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[48] R. Utsumi,et al. Inhibitors targeting two-component signal transduction. , 2008, Advances in experimental medicine and biology.
[49] J. S. Parkinson,et al. Bacterial chemoreceptors: high-performance signaling in networked arrays. , 2008, Trends in biochemical sciences.
[50] Gabriela Gonzalez-Bonet,et al. Reconstruction of the chemotaxis receptor–kinase assembly , 2006, Nature Structural &Molecular Biology.
[51] C. Clevenger. Signal transduction. , 2003, Breast disease.
[52] Christine Josenhans,et al. The role of motility as a virulence factor in bacteria. , 2002, International journal of medical microbiology : IJMM.
[53] M. Simon,et al. Nucleotide binding by the histidine kinase CheA , 2001, Nature Structural Biology.
[54] C D Kroenke,et al. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. , 2001, Methods in enzymology.
[55] M. Jain. Going against the Grain , 1996 .
[56] L. Kay,et al. Measurement of Slow ( μ sms ) Time Scale Dynamics in Protein Side Chains by 15 N Relaxation Dispersion NMR Spectroscopy : Application to Asn and Gln Residues in a Cavity Mutant of T 4 Lysozyme , 2022 .