Mechanism of Filamentation-Induced Allosteric Activation of the SgrAI Endonuclease

Smarajit Polley, Dmitry Lyumkis, Nancy C. Horton

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1497-1507.e3
JournalStructure
Volume27
Issue number10
DOIs
StatePublished - Oct 1 2019

Fingerprint

Type II Site Specific Deoxyribonucleases
DNA Cleavage
DNA
Enzymes
endodeoxyribonuclease SgrAI

Keywords

  • allostery
  • cryo-EM
  • DNA binding
  • DNA sequence specificity
  • endonuclease
  • enzyme mechanism
  • filament-forming enzyme
  • indirect readout
  • protein filament
  • self-association

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Mechanism of Filamentation-Induced Allosteric Activation of the SgrAI Endonuclease. / Polley, Smarajit; Lyumkis, Dmitry; Horton, Nancy C.

In: Structure, Vol. 27, No. 10, 01.10.2019, p. 1497-1507.e3.

Research output: Contribution to journalArticle

Polley, Smarajit ; Lyumkis, Dmitry ; Horton, Nancy C. / Mechanism of Filamentation-Induced Allosteric Activation of the SgrAI Endonuclease. In: Structure. 2019 ; Vol. 27, No. 10. pp. 1497-1507.e3.
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