Analysis of periplasmic sensor domains from Anaeromyxobacter dehalogenans 2 CP ‐C: Structure of one sensor domain from a histidine kinase and another from a chemotaxis protein
- Biosciences Argonne National Laboratory 9700 South Cass Avenue Lemont Illinois 60439
- Biosciences Argonne National Laboratory 9700 South Cass Avenue Lemont Illinois 60439, Structural Biology Center Biosciences division Argonne National Laboratory Lemont Illinois 60439
- The Midwest Center for Structural Genomics Biosciences division Argonne National Laboratory 9700 South Cass Avenue Lemont Illinois 60439
- Biosciences Argonne National Laboratory 9700 South Cass Avenue Lemont Illinois 60439, The Midwest Center for Structural Genomics Biosciences division Argonne National Laboratory 9700 South Cass Avenue Lemont Illinois 60439
- Department of Molecular and Experimental Medicine The Scripps Research Institute 10550 N Torrey Pines Rd La Jolla California 92037
- Biosciences Argonne National Laboratory 9700 South Cass Avenue Lemont Illinois 60439, Structural Biology Center Biosciences division Argonne National Laboratory Lemont Illinois 60439, The Midwest Center for Structural Genomics Biosciences division Argonne National Laboratory 9700 South Cass Avenue Lemont Illinois 60439
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 .
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1634844
- Journal Information:
- MicrobiologyOpen, Journal Name: MicrobiologyOpen Vol. 2 Journal Issue: 5; ISSN 2045-8827
- Publisher:
- Wiley Blackwell (John Wiley & Sons)Copyright Statement
- Country of Publication:
- United Kingdom
- Language:
- English
Web of Science
Similar Records
Structures and solution properties of two novel periplasmic sensor domains with c-type heme from chemotaxis proteins of Geobacter sulfurreducens : implications for signal transduction.
Structural analyses reveal that