Life Sciences & Biotechnology
Title : | structural and functional studies on the role of the copper ATPases in heavy metal detoxification. |
Area of research : | Life Sciences & Biotechnology |
Focus area : | structural Biology |
Principal Investigator : | Dr. Aayatti Mallick, Indian Institute Education And Research (IIsER) Kolkata, West Bengal |
Timeline Start Year : | 2024 |
Timeline End Year : | 2026 |
Contact info : | aayattigupta@gmail.com |
Details
Executive Summary : | Heavy metal pollution is a significant issue due to industrialization, affecting water and soil resources, human health, and food chains. Metals like cadmium, mercury, silver, and lead can inhibit enzyme systems, disrupting cellular processes. Copper and zinc are vital micronutrients, but excessive exposure can lead to liver toxicity, anemia, and neurological defects. P1B-ATPases play a crucial role in metal homeostasis, transporting metal ions across membranes and facilitating metalloprotein biosynthesis and detoxification. In prokaryotes, they are essential for metalloprotein assembly and metal distribution. Cu+ ATPases export non-biological toxic heavy metals, and the liver is a major site for xenobiotic detoxification. P1B-type ATPases have a core structure with a long N-terminal tail with 70-aa independently folded domains with a conserved sequence motif CXXC. A bioinformatic sequence-based study found that GMDCXXC over the GMTCXXC metal binding motif is present in divalent cation translocating Cd2+ and Zn2+ ATPases, affecting the role of acidic residues in divalent cation binding. This study aims to explore the specific metal binding affinity to different P1B-ATPase subtypes and the role of acidic residues in divalent specific cation binding. |
Total Budget (INR): | |
Organizations involved