AI Article Synopsis
- Over 140 million people globally are affected by arsenic contamination in drinking water, which poses significant toxicity to humans.
- Arsenite and arsenate, inorganic forms of arsenic, can be used by some microbes as energy sources, highlighting a unique aspect of microbial respiration.
- The study reveals AioX and its related proteins function as key regulators in arsenic metabolism, with structural analysis showing specific adaptations in protein binding that influence selectivity between arsenite and arsenate, indicating a complex evolutionary relationship.
Article Abstract
Arsenic contamination of drinking water affects more than 140 million people worldwide. While toxic to humans, inorganic forms of arsenic (arsenite and arsenate), can be used as energy sources for microbial respiration. AioX and its orthologues (ArxX and ArrX) represent the first members of a new sub-family of periplasmic-binding proteins that serve as the first component of a signal transduction system, that's role is to positively regulate expression of arsenic metabolism enzymes. As determined by X-ray crystallography for AioX, arsenite binding only requires subtle conformational changes in protein structure, providing insights into protein-ligand interactions. The binding pocket of all orthologues is conserved but this alone is not sufficient for oxyanion selectivity, with proteins selectively binding either arsenite or arsenate. Phylogenetic evidence, clearly demonstrates that the regulatory proteins evolved together early in prokaryotic evolution and had a separate origin from the metabolic enzymes whose expression they regulate.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5908839 | PMC |
| http://dx.doi.org/10.1038/s41598-018-24591-w | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Molybdate uptake interplay with ROS tolerance modulates bacterial pathogenesis.
Sci Adv
January 2025
Center for Microbiome Research of Med-X Institute, Shaanxi Provincial Key Laboratory of Sepsis in Critical Care Medicine, The First Affiliated Hospital, Xi'an Jiaotong University, Xi'an 710061, China.
The rare metal element molybdenum functions as a cofactor in molybdoenzymes that are essential to life in almost all living things. Molybdate can be captured by the periplasmic substrate-binding protein ModA of ModABC transport system in bacteria. We demonstrate that ModA plays crucial roles in growth, multiple metabolic pathways, and ROS tolerance in .
View Article and Find Full Text PDFProbing ligand-induced conformational changes in an MFS transporter in vivo using site-directed PEGylation.
J Mol Biol
January 2025
Department of Chemistry and Biochemistry, California State University, San Bernardino, 5500 University Pkwy, San Bernardino, CA 92407, USA. Electronic address:
So far, site-directed alkylation (SDA) studies on transporters in the Major Facilitator Superfamily (MFS) are mostly performed at conditions different from the native cellular environment. In this study, using GFP-based site-directed PEGylation, ligand-induced conformational changes in the lactose permease of Escherichia coli (LacY), were examined in vivo for the first time. Accessibility/reactivity of single-Cys replacements in a Cys-less LacY-eGFP fusion background was tested using methoxy polyethylene glycol-maleimide-5K (mPEG-Mal-5K) in the absence or presence of a ligand, and the band-shift of the fusion upon PEGylation was detected by in-gel fluorescence.
View Article and Find Full Text PDFDeciphering the molecular basis of lipoprotein recognition and transport by LolCDE.
Signal Transduct Target Ther
December 2024
Department of Laboratory Medicine, State Key Laboratory of Biotherapy, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China.
Outer membrane (OM) lipoproteins serve vital roles in Gram-negative bacteria, contributing to their pathogenicity and drug resistance. For these lipoproteins to function, they must be transported from the inner membrane (IM), where they are assembled, to the OM by the ABC transporter LolCDE. We have previously captured structural snapshots of LolCDE in multiple states, revealing its dynamic conformational changes.
View Article and Find Full Text PDFBiomimetic Pseudopeptides to Decipher the Interplay between Cu and Methionine-Rich Domains in Proteins.
Chemistry
December 2024
Univ. Grenoble Alpes, CEA, CNRS, Grenoble INP, IRIG, SyMMES, 38000, Grenoble, France.
Maintaining tightly copper homeostasis is crucial for the survival of all living organisms, in particular microorganisms like bacteria. They have evolved a number of proteins to capture, transport and deliver Cu(I), while avoiding Fenton-like reactions. Some Cu proteins exhibit methionine-rich (Met-rich) domains, whose role remains elusive.
View Article and Find Full Text PDFComparative proteomic analysis to annotate the structural association of the hypothetical proteins from the conserved domain of P. aeruginosa as novel vaccine candidates.
Biotechnol Lett
December 2024
Department of Bioinformatics, BioNome, Bengaluru, Karnataka, 560043, India.
Objectives: Pseudomonas aeruginosa, identified as an ESKAPE pathogen, contributes to severe clinical diseases worldwide and despite its prevalence an effective vaccine or treatment remains elusive. Numerous computational methods are being employed to target hypothetical proteins (HPs). Presently, no studies have predicted multi-epitope vaccines for these HPs.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!