This title appears in the Scientific Report :
2003
Please use the identifier:
http://dx.doi.org/10.1074/jbc.M305864200 in citations.
Please use the identifier: http://hdl.handle.net/2128/2824 in citations.
The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain
The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain
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...
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Personal Name(s): | Reinelt, S. |
---|---|
Hofmann, E. / Gerharz, T. / Bott, M. / Madden, D. R. | |
Contributing Institute: |
Biotechnologie 1; IBT-1 |
Published in: | The @journal of biological chemistry, 278 (2003) S. 39189 - 39196 |
Imprint: |
Bethesda, Md.
Soc.
2003
|
Physical Description: |
39189 - 39196 |
PubMed ID: |
12867417 |
DOI: |
10.1074/jbc.M305864200 |
Document Type: |
Journal Article |
Research Program: |
Biotechnologie |
Series Title: |
Journal of Biological Chemistry
278 |
Subject (ZB): | |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/2824 in citations.
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. |