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

Structure of HsdS subunit from Thermoanaerobacter tengcongensis sheds lights on mechanism of dynamic opening and closing of type I methyltransferase.

PloS one - 2 Mar 2011

Gao Pu, Tang Qun, An XiaoMin, Yan XiaoXue, Liang DongCai

Abstract excerpt

Type I DNA methyltransferases contain one specificity subunit (HsdS) and two modification subunits (HsdM). The electron microscopy model of M.EcoKI-M₂S₁ methyltransferase shows a reasonable closed state of this clamp-like enzyme, but the structure of the open state is still unclear. The 1.95 Å crystal structure of the specificity subunit from Thermoanaerobacter tengcongensis (TTE-HsdS) shows an unreported open...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA, Bacterial

Share to DNA Restriction-Modification Enzymes

Share to Methyltransferases

Share to Models, Molecular

Share to Protein Conformation

Share to Protein Subunits

Source

Open in PubMed Open full text

Identifiers

PMID: 21399684
DOI: 10.1371/journal.pone.0017346
PMCID: PMC3047542

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of HsdS subunit from Thermoanaerobacter tengcongensis sheds lights on mechanism of dynamic opening and closing of type I methyltransferase.PMID 21399684Read ↗

Structural insights into assembly, operation and inhibition of a type I restriction-modification system.Semantic proximity Read ↗

DndEi Exhibits Helicase Activity Essential for DNA Phosphorothioate Modification and ATPase Activity Strongly Stimulated by DNA Substrate with a GAAC/GTTC Motif.Semantic proximity Read ↗

5-methylcytosine-sensitive variants of Thermococcus kodakaraensis DNA polymerase.Semantic proximity Read ↗

The structure and function of MCM from archaeal M. Thermoautotrophicum.Semantic proximity Read ↗

A novel Mre11 protein from the hyperthermophilic euryarchaeon Thermococcus barophilus Ch5 possesses 5'-3' exonuclease and endonuclease activities.Semantic proximity Read ↗

Structural model for the multisubunit Type IC restriction-modification DNA methyltransferase M.EcoR124I in complex with DNA.Semantic proximity Read ↗

Distal Mutations in the β-Clamp of DNA Polymerase III* Disrupt DNA Orientation and Affect Exonuclease Activity.Semantic proximity Read ↗

Structural mechanism for coordination of proofreading and polymerase activities in archaeal DNA polymerases.Semantic proximity Read ↗

Functional evaluation of four putative DNA-binding regions in Thermoanaerobacter tengcongensis reverse gyrase.Semantic proximity Read ↗

Structural basis for substrate recognition and processive cleavage mechanisms of the trimeric exonuclease PhoExo I.Semantic proximity Read ↗

Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specificity.Semantic proximity Read ↗

Structure and activity of a thermostable thymine-DNA glycosylase: evidence for base twisting to remove mismatched normal DNA bases.Semantic proximity Read ↗

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