Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction

Nitrogen metabolism in bacteria and archaea is regulated by a ubiquitous class of proteins belonging to the PIIfamily. PII proteins act as sensors of cellular nitrogen, carbon, and energy levels, and they control the activities of a wide range of target proteins by protein-protein interaction. The s...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2011-11, Vol.108 (47), p.18972-18976
Hauptverfasser:	Rajendran, Chitra, Gerhardt, Edileusa C. M, Bjelic, Sasa, Gasperina, Antonietta, Scarduelli, Marcelo, Pedrosa, Fábio O, Chubatsu, Leda S, Merrick, Mike, Souza, Emanuel M, Winkler, Fritz K, Huergo, Luciano F, Li, Xiao-Dan
Format:	Artikel
Sprache:	eng
Schlagworte:	adenosine diphosphate adenosine triphosphate ammonia Archaea Azospirillum brasilense Azospirillum brasilense - enzymology Bacteria Bacterial proteins Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological Sciences Biological Transport - physiology carbon Cation Transport Proteins - metabolism Cell Membrane - metabolism cell membranes Crystal structure Crystallization cytoplasm energy Enzymes Gene expression regulation Metabolism Models, Molecular Molecular structure Monomers Multiprotein Complexes - chemistry Multiprotein Complexes - genetics Multiprotein Complexes - metabolism Mutagenesis, Site-Directed Nitrogen Nitrogen - metabolism Nitrogenase - metabolism Physiological regulation PII Nitrogen Regulatory Proteins - chemistry PII Nitrogen Regulatory Proteins - genetics PII Nitrogen Regulatory Proteins - metabolism post-translational modification Protein Conformation protein-protein interactions Proteins Quaternary ammonium compounds Quaternary Ammonium Compounds - metabolism site-directed mutagenesis Trimers
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