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          Institute: MPI für medizinische Forschung     Collection: Max-Planck-Forschungsgruppe Ionenkanalstruktur (Dean R. Madden)     Display Documents



ID: 125107.0, MPI für medizinische Forschung / Max-Planck-Forschungsgruppe Ionenkanalstruktur (Dean R. Madden)
The Structure of the Periplasmic Ligand-binding Domain of the Sensor Kinase CitA Reveals the First Extracellular PAS Domain
Authors:Reinelt, Stefan; Hofmann, Eckhard; Gerharz, Tanja; Bott, Michael; Madden, Dean R.
Language:English
Date of Publication (YYYY-MM-DD):2003-10-03
Title of Journal:Journal of Biological Chemistry
Journal Abbrev.:J. Biol. Chem.
Volume:278
Issue / Number:40
Start Page:39189
End Page:39196
Copyright:Copyright © 2003 by the American Society for Biochemistry and Molecular Biology
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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.
Free Keywords:CitAP, CitA periplasmic domain; MES, 2-[N-morpholino]ethanesulfonic acid; NCS, non-crystallographic symmetry; SeMet, selenomethionine; PYP, photoactive yellow protein
Comment of the Author/Creator:We gratefully acknowledge the assistance of N. Fehrmann (HTS Lab, Hauptmann-Woodward Institute, Buffalo, NY) in performing high-throughput crystallization screens. We acknowledge the Department of Biophysics (MPIMF) and the European Synchrotron Radiation Facility (Grenoble, France) for provision of X-ray diffraction facilities. We thank Dr. J. McCarthy for assistance in the use of ESRF beamline ID14-4 and Drs. J. Fethiere (EMBL, Heidelberg) and W. Kabsch (MPIMF) for assistance with data collection and analysis.
Last Change of the Resource (YYYY-MM-DD):2003-07-10
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Nachwuchsgruppe Ion Channel Structure
External Affiliations:Ruhr-Universität Bochum, Proteinkristallographie, Lehrstuhl für Biophysik D-44780 Bochum, Germany; Institut für Biotechnologie 1, Forschungszentrum Jülich, D-52425 Jülich, Germany; Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755-3844
Relations:-URI:http://jb.asm.org/cgi/content/full/186/6/1879
-URI:http://jb.asm.org/cgi/content/full/186/6/1694
-URI:http://www.ejbiochem.org/cgi/content/full/271/6/1198
-URI:http://www.jbc.org/cgi/ijlink?linkType=ABST&journalCode=plantcell&resid=14/5/1067
Identifiers:URI:http://www.jbc.org/cgi/content/abstract/278/40/391... [Abstract HTML]
URI:http://www.jbc.org/cgi/content/full/278/40/39189 [Fulltext HTML]
URI:http://www.jbc.org/cgi/reprint/278/40/39189 [Fulltext PDF]
DOI:10.1074/jbc.M305864200
LOCALID:6017 [PUMA publication management ID]
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