Abstract
The 3.5-Å cryo-EM structure of the filament formed by the type II restriction endonuclease SgrAI bound to DNA described in Polley et al. reveals the relevance of indirect readout for enzyme activity and a mechanism for filament-induced activation of DNA cleavage.
Original language | English (US) |
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Pages (from-to) | 1497-1507.e3 |
Journal | Structure |
Volume | 27 |
Issue number | 10 |
DOIs | |
State | Published - Oct 1 2019 |
Keywords
- DNA binding
- DNA sequence specificity
- allostery
- cryo-EM
- endonuclease
- enzyme mechanism
- filament-forming enzyme
- indirect readout
- protein filament
- self-association
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
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Dive into the research topics of 'Mechanism of Filamentation-Induced Allosteric Activation of the SgrAI Endonuclease'. Together they form a unique fingerprint.Datasets
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Structure of a DNA-bound dimer extracted from filamentous SgrAI endonuclease in its activated form
Polley, S. (Contributor), Lyumkis, D. (Contributor) & Horton, N. C. (Contributor), Protein Data Bank (PDB), Feb 26 2020
DOI: 10.2210/pdb6OBJ/pdb, https://www.wwpdb.org/pdb?id=pdb_00006obj
Dataset