Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and thermodynamic basis for enhanced DNA binding by a promiscuous mutant EcoRI endonuclease.

Structure (London, England : 1993) - 1 Nov 2007

Sapienza Paul J, Rosenberg John M, Jen-Jacobson Linda

Abstract excerpt

Promiscuous mutant EcoRI endonucleases bind to the canonical site GAATTC more tightly than does the wild-type endonuclease, yet cleave variant (EcoRI(*)) sites more rapidly than does wild-type. The crystal structure of the A138T promiscuous mutant homodimer in complex with a GAATTC site is nearly identical to that of the wild-type complex, except that the Thr138 side chains make packing interactions with bases in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Crystallography, X-Ray
Share to Deoxyribonuclease EcoRI

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Models, Molecular

Share to Nucleic Acid Conformation

Share to Protein Structure, Tertiary

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 17997963
DOI: 10.1016/j.str.2007.09.014
PMCID: PMC3366113

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and thermodynamic basis for enhanced DNA binding by a promiscuous mutant EcoRI endonuclease.PMID 17997963Read ↗

Thermodynamic and kinetic basis for the relaxed DNA sequence specificity of "promiscuous" mutant EcoRI endonucleases.Semantic proximity Read ↗

Temperature-sensitive mutants of the EcoRI endonuclease.Semantic proximity Read ↗

Free energy calculations and molecular dynamics simulations of wild-type and variants of the DNA-EcoRI complex.Semantic proximity Read ↗

Dynamics and thermodynamics of water around EcoRI bound to a minimally mutated DNA chain.Semantic proximity Read ↗

Imaging DNA loops induced by restriction endonuclease EcoRII. A single amino acid substitution uncouples target recognition from cooperative DNA interaction and cleavage.Semantic proximity Read ↗

Differential stabilization of reaction intermediates: specificity checkpoints for M.EcoRI revealed by transient fluorescence and fluorescence lifetime studies.Semantic proximity Read ↗

A monomeric mutant of restriction endonuclease EcoRI nicks DNA without sequence specificity.Semantic proximity Read ↗

Crystal structures of type II restriction endonuclease EcoO109I and its complex with cognate DNA.Semantic proximity Read ↗

Mutations in the alpha8 loop of human APE1 alter binding and cleavage of DNA containing an abasic site.Semantic proximity Read ↗

Direct monitoring of allosteric recognition of type IIE restriction endonuclease EcoRII.Semantic proximity Read ↗

Conformational flexibility in T4 endonuclease VII revealed by crystallography: implications for substrate binding and cleavage.Semantic proximity Read ↗

Pausing of the restriction endonuclease EcoRI during linear diffusion on DNA.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.