NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ

Bacteria live in capricious environments, in which they must continuously sense external conditions in order to adjust their shape, motility and physiology 1 . The histidine–aspartate phosphorelay signal-transduction system (also known as the two-component system) is important in cellular adaptation...

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Bibliographic Details
Published in:	Nature (London) Vol. 396; no. 6706; pp. 88 - 92
Main Authors:	Tanaka, Toshiyuki, Saha, Soumitra K., Tomomori, Chieri, Ishima, Rieko, Liu, Dingjiang, Tong, Kit I., Park, Heiyoung, Dutta, Rinku, Qin, Ling, Swindells, Mark B., Yamazaki, Toshimasa, Ono, Akira M., Kainosho, Masatsune, Inouye, Masayori, Ikura, Mitsuhiko
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 05.11.1998 Nature Publishing Nature Publishing Group
Subjects:	Amino Acid Sequence Bacteria Bacterial Outer Membrane Proteins - chemistry Bacteriology Biochemistry Biological and medical sciences Catalytic Domain Crystallography, X-Ray E coli Environmental changes Escherichia coli - chemistry Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Histidine Kinase Humanities and Social Sciences letter Magnetic Resonance Spectroscopy Microbiology Models, Molecular Molecular Sequence Data Morphology, structure, chemical composition multidisciplinary Multienzyme Complexes NMR Nuclear magnetic resonance Physiology Protein Conformation Protein Kinases - chemistry Proteins Recombinant Proteins - chemistry Residues Science Science (multidisciplinary) Transducers Transmembrane protein Enzymatic activity Molecular structure Enzyme Protein kinase Transferases Escherichia coli Bacteria NMR spectrometry Molecular domain Enterobacteriaceae
ISSN:	0028-0836, 1476-4687
Online Access:	Get full text
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