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
Open Access
- 30 July 2013
- journal article
- research article
- Published by Wiley in Microbiologyopen
- Vol. 2 (5), 766-777
- https://doi.org/10.1002/mbo3.112
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.Keywords
Funding Information
- U.S. Department of Energy Office of Biological and Environmental Research program (DE-AC02-06CH11357)
- division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy program (DE-AC02-06CH11357)
- National Institutes of Health (GM094585, GM019416)
- Argonne National Laboratory
This publication has 49 references indexed in Scilit:
- Two-component signal transductionCurrent Opinion in Microbiology, 2010
- Heme Binding to the Mammalian Circadian Clock Protein Period 2 Is NonspecificBiochemistry, 2010
- Comprehensive proteome profiling of the Fe(III)‐reducing myxobacterium Anaeromyxobacter dehalogenans 2CP‐C during growth with fumarate and ferric citrateProteomics, 2010
- The Physiological Stimulus for the BarA Sensor KinaseJournal of Bacteriology, 2010
- Extracytoplasmic PAS-Like Domains Are Common in Signal Transduction ProteinsJournal of Bacteriology, 2010
- PHENIX: a comprehensive Python-based system for macromolecular structure solutionActa Crystallographica Section D-Biological Crystallography, 2010
- Structural Analysis of Ligand Stimulation of the Histidine Kinase NarXStructure, 2009
- Cache – a signaling domain common to animal Ca2+-channel subunits and a class of prokaryotic chemotaxis receptorsTrends in Biochemical Sciences, 2000
- The three-dimensional structure of the aspartate receptor fromEscherichia coliActa Crystallographica Section D-Biological Crystallography, 1995
- Ligation-independent cloning of PCR products (LIC-PCR)Nucleic Acids Research, 1990