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

Solution structure of the catalytic domain of gammadelta resolvase. Implications for the mechanism of catalysis.

Journal of molecular biology - 27 Jul 2001

Pan B, Maciejewski M W, Marintchev A, Mullen G P

Abstract excerpt

The site-specific DNA recombinase, gammadelta resolvase, from Escherichia coli catalyzes recombination of res site-containing plasmid DNA to two catenated circular DNA products. The catalytic domain (residues 1-105), lacking a C-terminal dimerization interface, has been constructed and the NMR solution structure of the monomer determined. The RMSD of the NMR conformers for residues 2-92 excluding residues 37-45...

Read the complete abstract on PubMed

Topics

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

Share to Amides
Share to Catalysis
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Osmolar Concentration

Share to Recombinases

Share to Transposases

Source

Identifiers

PMID: 11501998
DOI: 10.1006/jmbi.2001.4821

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Solution structure of the catalytic domain of gammadelta resolvase. Implications for the mechanism of catalysis.PMID 11501998Read ↗

Secondary and tertiary structural changes in gamma delta resolvase: comparison of the wild-type enzyme, the I110R mutant, and the C-terminal DNA binding domain in solution.Semantic proximity Read ↗

The structure of Escherichia coli RusA endonuclease reveals a new Holliday junction DNA binding fold.Semantic proximity Read ↗

Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces.Semantic proximity Read ↗

Structure of a synaptic gammadelta resolvase tetramer covalently linked to two cleaved DNAs.Semantic proximity Read ↗

Two basic residues, Lys-107 and Lys-118, of RuvC resolvase are involved in critical contacts with the Holliday junction for its resolution.Semantic proximity Read ↗

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

Folded monomer of HIV-1 protease.Semantic proximity Read ↗

Origin of conformational dynamics in a globular protein.Semantic proximity Read ↗

Major groove recognition by three-stranded beta-sheets: affinity determinants and conserved structural features.Semantic proximity Read ↗

Cooperative binding of Tn3 resolvase monomers to a functionally asymmetric binding site.Semantic proximity Read ↗

Site-specific recombination in mammalian cells catalyzed by gammadelta resolvase mutants: implications for the topology of episomal DNA.Semantic proximity Read ↗

Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA holliday junction resolvase.Semantic proximity Read ↗

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