The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain
| Autor: | Stephan Reinelt, Michael Bott, Eckhard Hofmann, Dean R. Madden, Tanja Gerharz |
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| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Cytoplasm Protein Conformation Molecular Sequence Data chemistry [Protein Kinases] Biology Crystallography X-Ray Ligands Biochemistry Protein Structure Secondary Protein structure chemistry [Escherichia coli Proteins] PAS domain ddc:570 Escherichia coli Amino Acid Sequence Structural motif Molecular Biology Protein secondary structure metabolism [Cytoplasm] Chromatography Binding Sites Escherichia coli Proteins enzymology [Klebsiella pneumoniae] Cell Biology Periplasmic space Ligand (biochemistry) Protein Structure Tertiary dpiB protein E coli Klebsiella pneumoniae Transmembrane domain Periplasm enzymology [Periplasm] Biophysics metabolism [Escherichia coli] Signal transduction Dimerization Protein Kinases Protein Binding Signal Transduction |
| Zdroj: | The journal of biological chemistry 278, 39189-39196 (2003). doi:10.1074/jbc.M305864200 The Journal of Biological Chemistry |
| DOI: | 10.1074/jbc.M305864200 |
| Popis: | The integral membrane sensor kinase CitA of Klebsiella pneumoniae is part of a two-component signal transduction system that regulates the transport and metabolism of citrate in response to its environmental concentration. Two-component systems are widely used by bacteria for such adaptive processes, but the stereochemistry of periplasmic ligand binding and the mechanism of signal transduction across the membrane remain poorly understood. The crystal structure of the CitAP periplasmic sensor domain in complex with citrate reveals a PAS fold, a versatile ligand-binding structural motif that has not previously been observed outside the cytoplasm or implicated in the transduction of conformational signals across the membrane. Citrate is bound in a pocket that is shared among many PAS domains but that shows structural variation according to the nature of the bound ligand. In CitAP, some of the citrate contact residues are located in the final strand of the central beta-sheet, which is connected to the C-terminal transmembrane helix. These secondary structure elements thus provide a potential conformational link between the periplasmic ligand binding site and the cytoplasmic signaling domains of the receptor. |
| Databáze: | OpenAIRE |
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