A5073697126- Trace Elements in Health
- Metal complexes synthesis and properties
- Drug Transport and Resistance Mechanisms
- Enzyme Structure and Function
- Protein Structure and Dynamics
- Photoreceptor and optogenetics research
- Metabolism, Diabetes, and Cancer
- Photosynthetic Processes and Mechanisms
- Computational Drug Discovery Methods
- Protein Kinase Regulation and GTPase Signaling
- ATP Synthase and ATPases Research
- Lipid Membrane Structure and Behavior
- Amino Acid Enzymes and Metabolism
- Cytokine Signaling Pathways and Interactions
- Ubiquitin and proteasome pathways
- Advanced NMR Techniques and Applications
- Neuroscience and Neuropharmacology Research
- Metabolism and Genetic Disorders
- Spectroscopy and Quantum Chemical Studies
- Metabolomics and Mass Spectrometry Studies
- Cellular transport and secretion
- Bacterial Genetics and Biotechnology
- Microbial Inactivation Methods
- Advanced MRI Techniques and Applications
Umeå University
2021-2024
Abstract Copper transporting P-type (P 1B-1 -) ATPases are essential for cellular homeostasis. Nonetheless, the E1-E1P-E2P-E2 states mechanism of P -ATPases remains poorly understood. In particular, role intrinsic metal binding domains (MBDs) is enigmatic. Here, four cryo-EM structures and molecular dynamics simulations a -ATPase combined to reveal that in many eukaryotes MBD immediately prior ATPase core, −1 , serves structural role, remodeling ion-uptake region. contrast, −2 likely assists...
Time-resolved x-ray solution scattering identifies cooperative structural dynamics in the adenylate kinase enzymatic reaction.
Abstract Copper is essential for living cells, yet toxic at elevated concentrations. Class 1B P-type (P -) ATPases are present in all kingdoms of life, facilitating cellular export transition metals including copper. follow an alternating access mechanism, with inward-facing E1 and outward-facing E2 conformations. Nevertheless, no structural information on states available P -ATPases, hampering mechanistic understanding. Here, we structures that reach 2.7 Å resolution a copper-specific...
Calcium (Ca 2+ ) signaling is fundamental to cellular processes in both eukaryotic and prokaryotic organisms. While the mechanisms underlying Ca transport are well documented, an understanding of remains nascent. LMCA1, a adenosine triphosphatase (ATPase) from Listeria monocytogenes , has emerged as prototype for elucidating structure dynamics transport. Here, we used multidisciplinary approach integrating kinetics, structure, unravel intricacies LMCA1 function. A cryo–electron microscopy...
ATP7B is a human copper-transporting P1B-type ATPase that involved in copper homeostasis and resistance to platinum drugs cancer cells. consists of core regulatory N-terminal tail contains six metal-binding domains (MBD1-6) connected by linker regions. The MBDs can bind copper, which changes the dynamics domain activates protein, but underlying mechanism remains unknown. To identify possible copper-specific structural transport regulation, we constructed model spanning catalytic performed...
Protein dynamics are essential to biological function, and methods determine such structural rearrangements constitute a frontier in biology. Synchrotron radiation can track real-time protein dynamics, but accessibility dedicated high-flux single X-ray pulse time-resolved beamlines is scarce targets amendable characterization limited. These limitations be alleviated by triggering the reaction laser-induced activation of caged compound probing fast-readout detectors. In this work, we...
Abstract ATP7B is a human copper-transporting P 1B -type ATPase that involved in copper homeostasis and resistance to platinum drugs cancer cells. consists of core regulatory N-terminal tail contains six metal-binding domains (MBD1-6) connected by linker regions. The MBDs can bind copper, which changes the dynamics domain activates protein, but underlying mechanism remains unknown. To identify possible copper-specific structural transport regulation, we constructed model spanning catalytic...