1p0z
From Proteopedia
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Sensor Kinase CitA binding domain
Overview
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.
About this Structure
1P0Z is a Single protein structure of sequence from Klebsiella pneumoniae with FLC, NA, MO7 and OMO as ligands. Active as Histidine kinase, with EC number 2.7.13.3 Full crystallographic information is available from OCA.
Reference
The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain., Reinelt S, Hofmann E, Gerharz T, Bott M, Madden DR, J Biol Chem. 2003 Oct 3;278(40):39189-96. Epub 2003 Jul 16. PMID:12867417
Page seeded by OCA on Tue Nov 20 23:21:44 2007
Categories: Histidine kinase | Klebsiella pneumoniae | Single protein | Bott, M. | Gerharz, T. | Hofmann, E. | Madden, D.R. | Reinelt, S. | FLC | MO7 | NA | OMO | Kinase | Transferase
