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Crystal structure of the anti-CRISPR protein AcrIE7.
Biochem Biophys Res Commun
January 2025
Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, 300070, China; Department of Pharmacology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, 300070, China. Electronic address:
Bacterial adaptive immunity, driven by CRISPR-Cas systems, protects against foreign nucleic acids from mobile genetic elements (MGEs), like bacteriophages. The type I-E CRISPR-Cas system employs the Cascade (CRISPR-associated complex for antiviral defense) complex for target DNA cleavage, guided by crRNA. Anti-CRISPR (Acr) proteins, such as AcrIE7, counteract this defense by inhibiting Cascade activity.
View Article and Find Full Text PDFProtein binding and folding through an evolutionary lens.
Curr Opin Struct Biol
January 2025
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, SE-75123 Uppsala, Sweden. Electronic address:
Protein-protein associations are often mediated by an intrinsically disordered protein region interacting with a folded domain in a coupled binding and folding reaction. Classic physical organic chemistry approaches together with structural biology have shed light on mechanistic aspects of such reactions. Further insight into general principles may be obtained by interpreting the results through an evolutionary lens.
View Article and Find Full Text PDFProbing the functional constraints of influenza A virus NEP by deep mutational scanning.
Cell Rep
January 2025
Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA; Carl R. Woese Institute for Genomic Biology, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA; Center for Biophysics and Quantitative Biology, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA; Carle Illinois College of Medicine, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA. Electronic address:
The influenza A virus nuclear export protein (NEP) is a multifunctional protein that is essential for the viral life cycle and has very high sequence conservation. However, since the open reading frame of NEP largely overlaps with that of another influenza viral protein, non-structural protein 1, it is difficult to infer the functional constraints of NEP based on sequence conservation analysis. In addition, the N-terminal of NEP is structurally disordered, which further complicates the understanding of its function.
View Article and Find Full Text PDFInterlayer Spacing Optimization Combined with Zinc-Philic Engineering Fostering Efficient Zn Storage of VCT MXenes for Aqueous Zinc-Ion Batteries.
Small
January 2025
School of Physics and Materials Science, Nanchang University, Nanchang, Jiangxi, 330031, China.
As emerging cutting-edge energy storage technologies, aqueous zinc-ion batteries (AZIBs) have garnered extensive research attention for its high safety, low cost, abundant raw materials, and, eco-friendliness. Nevertheless, the commercialization of AZIBs is mainly limited by insufficient development of cathode materials. Among potential candidates, MXene-based materials stand out as a promising option for their unique combination of hydrophilicity and conductivity.
View Article and Find Full Text PDFStructure of the T=13 capsid of infectious pancreatic necrosis virus (IPNV)-a salmonid birnavirus.
J Virol
January 2025
Laboratory of Molecular Biophysics, Department of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden.
Birnaviruses infect a broad range of vertebrate hosts, including fish and birds, and cause substantial economic losses in the fishery and livestock industries. The infectious pancreatic necrosis virus (IPNV), an aquabirnavirus, specifically infects salmonids. While structures on T=1 subviral particles of the birnaviruses, including IPNV, have been studied, structural insights into the infectious T=13 particles have been limited to the infectious bursal disease virus (IBDV), an avibirnavirus.
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