title: Analysis of periplasmic sensor domains from Anaeromyxobacter dehalogenans 2CP-C: structure of one sensor domain from a histidine kinase and another from a chemotaxis protein.
abstract: Anaeromyxobacter dehalogenans is a δ-proteobacterium found in diverse soils and sediments. It is of interest in bioremediation efforts due to its dechlorination and metal-reducing capabilities. To gain an understanding on A. dehalogenans' abilities to adapt to diverse environments we analyzed its signal transduction proteins. The A. dehalogenans genome codes for a large number of sensor histidine kinases (HK) and methyl-accepting chemotaxis proteins (MCP); among these 23 HK and 11 MCP proteins have a sensor domain in the periplasm. These proteins most likely contribute to adaptation to the organism's surroundings. We predicted their three-dimensional folds and determined the structures of two of the periplasmic sensor domains by X-ray diffraction. Most of the domains are predicted to have either PAS-like or helical bundle structures, with two predicted to have solute-binding protein fold, and another predicted to have a 6-phosphogluconolactonase like fold. Atomic structures of two sensor domains confirmed the respective fold predictions. The Adeh_2942 sensor (HK) was found to have a helical bundle structure, and the Adeh_3718 sensor (MCP) has a PAS-like structure. Interestingly, the Adeh_3718 sensor has an acetate moiety bound in a binding site typical for PAS-like domains. Future work is needed to determine whether Adeh_3718 is involved in acetate sensing by A. dehalogenans.
authors.affiliation: Biosciences, Argonne National Laboratory, 9700 South Cass Avenue, Lemont, Illinois, 60439.
authors.forename: P Raj
authors.initials: PR
authors.lastname: Pokkuluri
authors.forename: Jeff
authors.initials: J
authors.lastname: Dwulit-Smith
authors.forename: Norma E
authors.initials: NE
authors.lastname: Duke
authors.forename: Rosemarie
authors.initials: R
authors.lastname: Wilton
authors.forename: Jamey C
authors.initials: JC
authors.lastname: Mack
authors.forename: Jessica
authors.initials: J
authors.lastname: Bearden
authors.forename: Ella
authors.initials: E
authors.lastname: Rakowski
authors.forename: Gyorgy
authors.initials: G
authors.lastname: Babnigg
authors.forename: Hendrik
authors.initials: H
authors.lastname: Szurmant
authors.forename: Andrzej
authors.initials: A
authors.lastname: Joachimiak
authors.forename: Marianne
authors.initials: M
authors.lastname: Schiffer
mesh_terms: D019342:Acetic Acid / Q000737:chemistry; D000222:Adaptation, Physiological; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D000071677:Histidine Kinase; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D009231:Myxococcales / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019897:Periplasm / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D011494:Protein Kinases / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D015398:Signal Transduction; D040681:Structural Homology, Protein
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D011994:Recombinant Proteins; D011494:Protein Kinases; D000071677:Histidine Kinase; D019342:Acetic Acid
keywords: Acetate; PAS-like; chemotaxis; helical bundle; periplasmic sensor domains; sensor histidine kinase
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