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Título: | Conserved GTPase mechanism in bacterial FtsZ and archaeal tubulin filaments |
Autor: | Andreu, José Manuel CSIC ORCID ; Ruiz, Federico M. CSIC ORCID ; Fernández-Tornero, Carlos CSIC ORCID | Palabras clave: | FtsZ GTPase Evolution Mechanism Tubulin |
Fecha de publicación: | 8-nov-2022 | Editor: | John Wiley & Sons | Citación: | FEBS Journal (2022) | Resumen: | Self-assembling protein filaments are at the heart of cell function. Among them, tubulin-like proteins are essential for cell division, DNA segregation and cytoskeletal functions across the domains of life. FtsZ and tubulin share their core structures, a characteristic nucleotide-binding pocket and similar protofilament architecture. GTP hydrolysis between consecutive subunits drives their assembly dynamics. Two recent studies provide previously missing, filament atomic structures of bacterial FtsZ and a recently discovered archaeal tubulin in their nucleotide triphosphate-bound states. Both filament structures reveal strikingly conserved interfacial GTPase active sites, with Mg2+ and K+ /Na+ cations and an NxDxxD/E triad of catalytic residues, probably inherited from the common ancestor of FtsZs and tubulins. Moreover, both proteins exhibit nucleotide-regulated subunit association mediated by interfacial water bridges, as well as polymerization-induced structural changes, likely enabling related dynamic assembly mechanisms. | Descripción: | 6 p.-2 fig. | Versión del editor: | https://doi.org/10.1111/febs.16675 | URI: | http://hdl.handle.net/10261/285359 | DOI: | 10.1111/febs.16675 | ISSN: | 1742-464X | E-ISSN: | 1742-4658 |
Aparece en las colecciones: | (CIB) Artículos |
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The FEBS Journal - 2022 - Andreu - Conserved GTPase mechanism in bacterial FtsZ and archaeal tubulin filaments.pdf | Artículo principal | 2,84 MB | Adobe PDF | Visualizar/Abrir |
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