D-loop Dynamics and Near-Atomic-Resolution Cryo-EM Structure of Phalloidin-Bound F-Actin
| العنوان: | D-loop Dynamics and Near-Atomic-Resolution Cryo-EM Structure of Phalloidin-Bound F-Actin |
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| المؤلفون: | Sanchaita Das, Zeynep A. Oztug Durer, Emil Reisler, Z. Hong Zhou, Peng Ge, Elena E. Grintsevich |
| المساهمون: | Acibadem University Dspace |
| المصدر: | Structure (London, England : 1993), vol 28, iss 5 Structure |
| بيانات النشر: | Elsevier BV, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | Models, Molecular, Phalloidine, Cryo-electron microscopy, Phalloidin, 1.1 Normal biological development and functioning, Mutant, high-resolution cryo-EM, Biophysics, Saccharomyces cerevisiae, macromolecular substances, Article, Protein filament, 03 medical and health sciences, chemistry.chemical_compound, Models, Underpinning research, Structural Biology, Information and Computing Sciences, Microscopy, Deoxyribonuclease I, Disulfides, Molecular Biology, Actin, 030304 developmental biology, F-actin structure, 0303 health sciences, Cryoelectron Microscopy, 030302 biochemistry & molecular biology, Dynamics (mechanics), Resolution (electron density), Molecular, Biological Sciences, chemical crosslinking, Actins, Cross-Linking Reagents, chemistry, Mutation, Chemical Sciences, Generic health relevance, D-loop dynamics |
| الوصف: | Detailed molecular information on G-actin assembly into filaments (F-actin), and their structure, dynamics, and interactions, is essential for understanding their cellular functions. Previous studies indicate that a flexible DNase I binding loop (D-loop, residues 40-50) plays a major role in actin's conformational dynamics. Phalloidin, a ``gold standard{''} for actin filament staining, stabilizes them and affects the D-loop. Using disulfide crosslinking in yeast actin D-loop mutant Q41C/V45C, light-scattering measurements, and cryoelectron microscopy reconstructions, we probed the constraints of D-loop dynamics and its contribution to F-actin formation/stability. Our data support a model of residues 41-45 distances that facilitate G- to F-actin transition. We report also a 3.3-angstrom resolution structure of phalloidin-bound F-actin in the ADP-Pi-like (ADP-BeFx) state. This shows the phalloidin-binding site on F-actin and how the relative movement between its two protofilaments is restricted by it. Together, our results provide molecular details of F-actin structure and D-loop dynamics. |
| وصف الملف: | application/pdf |
| تدمد: | 0969-2126 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e36180bf8f4fa5127376d14c57641dc6 https://doi.org/10.1016/j.str.2020.04.004 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....e36180bf8f4fa5127376d14c57641dc6 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 09692126 |
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