Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
Many important proteins undergo pH-dependent conformational changes resulting in "on-off" switches for protein function, which are essential for regulation of life processes and have wide application potential. Here, we report a pair of cellulosomal assembly modules, comprising a cohesin and a dockerin from , which interact together following a unique pH-dependent switch between two functional sites rather than on-off states. The two cohesin-binding sites on the dockerin are switched from one to the other at pH 4.8 and 7.5 with a 180° rotation of the bound dockerin. Combined analysis by nuclear magnetic resonance spectroscopy, crystal structure determination, mutagenesis, and isothermal titration calorimetry elucidates the chemical and structural mechanism of the pH-dependent switching of the binding sites. The pH-dependent dual-binding-site switch not only represents an elegant example of biological regulation but also provides a new approach for developing pH-dependent protein devices and biomaterials beyond an on-off switch for biotechnological applications.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7608827 | PMC |
| http://dx.doi.org/10.1126/sciadv.abd7182 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
A Mesoporous Silica-Based Naringenin Delivery System Promoting Macrophage M2 Polarization in Atherosclerosis.
Biomater Res
September 2025
Department of Vascular Surgery, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China.
Atherosclerosis is the leading cause of global cardiovascular morbidity and mortality associated with inflammatory and immunological mechanisms. Immunotherapy has demonstrated promising efficacy in the management of atherosclerosis. Nevertheless, certain immunotherapeutic approaches are associated with limitations, including suboptimal efficacy and non-negligible adverse effects.
View Article and Find Full Text PDFBreaking the reproducibility barrier with standardized protocols for plant-microbiome research.
PLoS Biol
September 2025
Environmental Genomics and Systems Biology, Lawrence Berkeley National Laboratory, Berkeley, California, United States of America.
Inter-laboratory replicability is crucial yet challenging in microbiome research. Leveraging microbiomes to promote soil health and plant growth requires understanding underlying molecular mechanisms using reproducible experimental systems. In a global collaborative effort involving five laboratories, we aimed to help advance reproducibility in microbiome studies by testing our ability to replicate synthetic community assembly experiments.
View Article and Find Full Text PDFState-Dependent Dynamic Communication Networks in a Pentameric Ligand-Gated Ion Channel.
J Phys Chem B
September 2025
School of Science, RMIT University, Melbourne 3000, Australia.
Pentameric ligand-gated ion channels control synaptic neurotransmission via an allosteric mechanism, whereby agonist binding induces global protein conformational changes that open an ion-conducting pore. For the proton-activated bacterial () ligand-gated ion channel (GLIC), high-resolution structures are available in multiple conformational states. We used a library of atomistic molecular dynamics (MD) simulations to study conformational changes and to perform dynamic network analysis to elucidate the communication pathways underlying the gating process.
View Article and Find Full Text PDFElevated acidity from natural and anthropogenic sources can be a significant stressor for plants, affecting essential processes such as nutrient uptake and growth. While low pH (< 4) is generally considered stressful for plants, differential impacts of distinct acid types-organic versus inorganic, strong versus weak-on plant growth and development remain unclear. To address this knowledge gap, we evaluated the responses of two Brassicaceae species to organic (acetic) and inorganic (hydrochloric, sulfuric) acids at three pH levels (pH 2.
View Article and Find Full Text PDFCathepsin K and glycosaminoglycans differentially regulate matrix metalloproteinase activity in dentin under various pH conditions.
Int J Biol Macromol
September 2025
Fujian Key Laboratory of Oral Diseases & Fujian Provincial Engineering Research Center of Oral Biomaterial & Stomatological Key Laboratory of Fujian College and University, School and Hospital of Stomatology, Fujian Medical University, Fuzhou, 350000, China; Research Center of Dental Esthetics and B
This study examined the pH-dependent (3, 5, and 7) regulation of matrix metalloproteinase (MMP) activity by cathepsin K (catK) and glycosaminoglycans (GAGs) using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), fluorescence assays, and human dentin slice experiments. The direct effects of catK were evaluated in the catK-active, catK-deficient, and odanacatib (ODN)-inhibited groups, whereas indirect GAG/ tissue inhibitor of metalloproteinase (TIMP)-mediated regulation was assessed in the catK-active, ODN-inhibited, and chondroitin sulfate (CS)-treated groups through dimethylmethylene blue (DMMB) assays, in situ zymography, and immunofluorescence staining. CatK directly activated MMP-2 (62 kDa) and MMP-9 (82 kDa) at all pH values, with no activation observed in the ODN-inhibited or catK-deficient groups.
View Article and Find Full Text PDF