ArticleActa crystallographica. Section D, Biological crystallography2011
New clues in the allosteric activation of DNA cleavage by SgrAI: structures of SgrAI bound to cleaved primary-site DNA and uncleaved secondary-site DNA.
Article in Acta crystallographica. Section D, Biological crystallography, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Two-metal ion mechanism of DNA cleavage by activated, filamentous SgrAI.The Journal of biological chemistry · 2024Article
- The role of filamentation in activation and DNA sequence specificity of the sequence-specific endonuclease SgrAI.Biochemical Society transactions · 2022Article
- Pretransition state and apo structures of the filament-forming enzyme SgrAI elucidate mechanisms of activation and substrate specificity.The Journal of biological chemistry · 2022Article
- Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation.Biophysical reviews · 2019Review
- Mechanism of Filamentation-Induced Allosteric Activation of the SgrAI Endonuclease.Structure (London, England : 1993) · 2019Article
- Unique mechanism of target recognition by PfoI restriction endonuclease of the CCGG-family.Nucleic acids research · 2019Article
- The run-on oligomer filament enzyme mechanism of SgrAI: Part 1. Assembly kinetics of the run-on oligomer filament.The Journal of biological chemistry · 2018Article
- The run-on oligomer filament enzyme mechanism of SgrAI: Part 2. Kinetic modeling of the full DNA cleavage pathway.The Journal of biological chemistry · 2018Article
- Probing the run-on oligomer of activated SgrAI bound to DNA.PloS one · 2015Article
- Allosteric regulation of DNA cleavage and sequence-specificity through run-on oligomerization.Structure (London, England : 1993) · 2013Article
- Structural analysis of activated SgrAI-DNA oligomers using ion mobility mass spectrometry.Biochemistry · 2013Article
- Activation of DNA cleavage by oligomerization of DNA-bound SgrAI.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
SgrAI is a type II restriction endonuclease that cuts an unusually long recognition sequence and exhibits allosteric self-activation with expansion of DNA-sequence specificity. The three-dimensional crystal structures of SgrAI bound to cleaved primary-site DNA and Mg²(+) and bound to secondary-site DNA with either Mg²(+) or Ca²(+) are presented. All three structures show a conformation of enzyme and DNA similar to the previously determined dimeric structure of SgrAI bound to uncleaved primary-site DNA and Ca²(+) [Dunten et al. (2008), Nucleic Acids Res. 36, 5405-5416], with the exception of the cleaved bond and a slight shifting of the DNA in the SgrAI/cleaved primary-site DNA/Mg²(+) structure. In addition, a new metal ion binding site is located in one of the two active sites in this structure, which is consistent with proposals for the existence of a metal-ion site near the 3'-O leaving group.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.