A5008120438- Iron Metabolism and Disorders
- Trace Elements in Health
- Plant Micronutrient Interactions and Effects
- X-ray Diffraction in Crystallography
- Crystallization and Solubility Studies
- Porphyrin Metabolism and Disorders
- Advanced X-ray Imaging Techniques
- Biofuel production and bioconversion
- RNA and protein synthesis mechanisms
- Microbial Metabolic Engineering and Bioproduction
- Hemoglobinopathies and Related Disorders
- Crystallography and Radiation Phenomena
- Enzyme Production and Characterization
- Metal and Thin Film Mechanics
- Metabolomics and Mass Spectrometry Studies
- Boron and Carbon Nanomaterials Research
- Pharmaceutical and Antibiotic Environmental Impacts
- Microbial Community Ecology and Physiology
- Fungal and yeast genetics research
- Mollusks and Parasites Studies
- Enzyme Structure and Function
- Molecular Biology Techniques and Applications
- Protein Structure and Dynamics
- Endoplasmic Reticulum Stress and Disease
- Protist diversity and phylogeny
University of Oxford
2019-2023
Discovery Centre
2023
University of Edinburgh
2014-2020
Science Oxford
2020
Genomics (United Kingdom)
2020
State Key Laboratory of Microbial Technology
2013-2019
Shandong University
2013-2019
Quantitative BioSciences
2016
Institute of Structural and Molecular Biology
2015
Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage. We have characterized the structure function of new member ferritin superfamily is sequestered an encapsulin capsid. show this encapsulated (EncFtn) has two main alpha helices, which assemble in metal dependent manner form ferroxidase center at dimer interface. EncFtn adopts open decameric topologically distinct other ferritins. While acts as ferroxidase, it cannot...
Ferritins are a large family of intracellular proteins that protect the cell from oxidative stress by catalytically converting Fe(II) into less toxic Fe(III) and storing iron minerals within their core. Encapsulated ferritins (EncFtn) sub-family ferritin-like proteins, which widely distributed in all bacterial archaeal phyla. The recently characterized Rhodospirillum rubrum EncFtn displays an unusual structure when compared with classical ferritins, open decameric is enzymatically active,...
Solute carriers (SLCs) are membrane transporters that import and export a range of endogenous exogenous substrates, including ions, nutrients, metabolites, neurotransmitters, pharmaceuticals. Despite having emerged as attractive therapeutic targets markers disease, this group proteins is still relatively underdrugged by current Drug discovery projects for these impeded limited structural, functional, physiological knowledge, ultimately due to the difficulties in expression purification class...
Encapsulated ferritins (EncFtn) are a recently characterised member of the ferritin superfamily. EncFtn proteins sequestered within encapsulin nanocompartments and form unique biological iron storage system. Here, we use native mass spectrometry hydrogen-deuterium exchange to elucidate metal-mediated assembly pathway EncFtn.
Encapsulated ferritins belong to the universally distributed ferritin superfamily, whose members function as iron detoxification and storage systems. have a distinct annular structure must associate with an encapsulin nanocage form competent store that is capable of holding significantly more than classical ferritins. The catalytic mechanism oxidation in family still open question because differences organization ferroxidase site neighboring secondary metal-binding sites. We previously...
Characterizing and engineering microbial communities for lignocellulosic biofuel production has received widespread attention. Previous research established that Clostridium thermocellum JN4 Thermoanaerobacterium thermosaccharolyticum GD17 coculture significantly improves overall cellulosic efficiency. Here, we investigated this interaction revealed the mechanism underlying improved efficiency observed. In contrast to previously reported mutualistic relationship, a harmful effect toward C....
Abstract Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage. We have characterized the structure function of new member ferritin superfamily is sequestered an encapsulin capsid. show this encapsulated (EncFtn) has two main alpha helices, which assemble in metal dependent manner form ferroxidase centre at dimer interface. EncFtn adopts open decameric topologically distinct other ferritins. While acts as ferroxidase, it...
Abstract Proline is widely known as the only proteogenic amino acid with a secondary amine. In addition to its crucial role in protein structure, modulates neurotransmission and regulates kinetics of signaling proteins. To understand structural basis proline import, we solved structure transporter SIT1 complex COVID-19 viral receptor ACE2 by cryo-electron microscopy. The pipecolate-bound reveals specific sequence requirements for transport SLC6 family how this excludes acids extended side...
ABSTRACT Iron is an essential element for many biological processes; however, due to its high reactivity iron can also be very toxic, producing reactive oxygen species through Fenton chemistry. Ferritins protect the cell from oxidative stress by catalytically converting Fe(II) into less toxic Fe(III) and storing resulting minerals within their core. Encapsulated ferritins (EncFtn) are a sub-family of ferritin-like proteins, which widely distributed in all bacterial archaeal phyla. We...