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Catalysis and structure of nitrogenases
Curr Opin Struct Biol. 2023 Oct 4;83:102719. doi: 10.1016/j.sbi.2023.102719. Online ahead of print.ABSTRACTIn providing bioavailable nitrogen as building blocks for all classes of biomacromolecules, biological nitrogen fixation is an essential process for all organismic life. Only a single enzyme, nitrogenase, performs this task at ambient conditions and with ATP as an energy source. The assembly of the complex iron-sulfur enzyme nitrogenase and its catalytic mechanism remains a matter of intense study. Recent progress in the structural analysis of the three known isoforms of nitrogenase-differentiated primarily by the het...
Source: Current Opinion in Structural Biology - October 6, 2023 Category: Biology Authors: Oliver Einsle Source Type: research

Editorial Overview: Protein-nucleic acid Interactions
Curr Opin Struct Biol. 2023 Oct 1;83:102708. doi: 10.1016/j.sbi.2023.102708. Online ahead of print.NO ABSTRACTPMID:37788517 | DOI:10.1016/j.sbi.2023.102708 (Source: Current Opinion in Structural Biology)
Source: Current Opinion in Structural Biology - October 3, 2023 Category: Biology Authors: James Berger Karl-Peter Hopfner Source Type: research

Viral amyloids: New opportunities for antiviral therapeutic strategies
Curr Opin Struct Biol. 2023 Sep 30;83:102706. doi: 10.1016/j.sbi.2023.102706. Online ahead of print.ABSTRACTAmyloidoses are an array of diseases associated with the aggregation of proteins into fibrils. While it was previously thought that amyloid fibril-forming proteins are exclusively host-cell encoded, recent studies have revealed that pathogenic viruses can form amyloid-like fibrils too. Intriguingly, viral amyloids are often composed of virulence factors, known for their contribution to cell death and disease progression. In this review, we survey the literature about viral proteins capable of forming amyloid-like fib...
Source: Current Opinion in Structural Biology - October 2, 2023 Category: Biology Authors: Frank Gondelaud Pierre-Yves Lozach Sonia Longhi Source Type: research

Protein disorder and autoinhibition: The role of multivalency and effective concentration
Curr Opin Struct Biol. 2023 Sep 29;83:102705. doi: 10.1016/j.sbi.2023.102705. Online ahead of print.ABSTRACTRegulation of protein binding through autoinhibition commonly occurs via interactions involving intrinsically disordered regions (IDRs). These intramolecular interactions can directly or allosterically inhibit intermolecular protein or DNA binding, regulate enzymatic activity, and control the assembly of large macromolecular complexes. Autoinhibitory interactions mediated by protein disorder are inherently transient, making their identification and characterization challenging. In this review, we explore the structur...
Source: Current Opinion in Structural Biology - October 1, 2023 Category: Biology Authors: Malissa Fenton Emily Gregory Gary Daughdrill Source Type: research

Folding and functions of knotted proteins
Curr Opin Struct Biol. 2023 Sep 29;83:102709. doi: 10.1016/j.sbi.2023.102709. Online ahead of print.ABSTRACTTopologically knotted proteins have entangled structural elements within their native structures that cannot be disentangled simply by pulling from the N- and C-termini. Systematic surveys have identified different types of knotted protein structures, constituting as much as 1% of the total entries within the Protein Data Bank. Many knotted proteins rely on their knotted structural elements to carry out evolutionarily conserved biological functions. Being knotted may also provide mechanical stability to withstand unf...
Source: Current Opinion in Structural Biology - October 1, 2023 Category: Biology Authors: Shang-Te Danny Hsu Source Type: research