Pin Lyu

ORCID: 0000-0003-4532-0430
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About
Contact & Profiles
Research Areas
  • Drug Transport and Resistance Mechanisms
  • Trace Elements in Health
  • Plant Micronutrient Interactions and Effects
  • Metal complexes synthesis and properties
  • ATP Synthase and ATPases Research
  • Ion Transport and Channel Regulation
  • Mitochondrial Function and Pathology

University of Copenhagen
2021-2024

Maersk (Denmark)
2022

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...

10.1038/s41467-022-32751-w article EN cc-by Nature Communications 2022-08-31

Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic excessive amounts. Heavy-metal transporting P-type (PIB) ATPases crucial for homeostasis, conferring cellular detoxification and redistribution through transport of these ions across membranes. No structural information is available the PIB-4-ATPases, subclass with broadest cargo scope, hence even their topology remains elusive. Here, we present structures complementary functional analyses...

10.7554/elife.73124 article EN cc-by eLife 2021-12-24

Copper is an essential micronutrient and yet highly toxic to cells at elevated concentrations. P 1B ‐ATPase proteins are critical for this regulation, providing active extrusion across cellular membranes. One unique molecular adaptation of ‐ATPases compared other P‐type ATPases the presence metal‐binding domains (MBDs) cytosolic termini, which however poorly characterized with elusive mechanistic role. Here we present MBD architecture in metal‐free metal‐bound forms archetype Cu + ‐specific...

10.1111/febs.17330 article EN cc-by FEBS Journal 2024-11-28
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