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

Hexameric RSF1010 helicase RepA: the structural and functional importance of single amino acid residues.

Nucleic acids research - 15 Oct 2003

Ziegelin Günter, Niedenzu Timo, Lurz Rudi, Saenger Wolfram, Lanka Erich

Abstract excerpt

In the known monoclinic crystals the 3-dimensional structure of the hexameric, replicative helicase RepA encoded by plasmid RSF1010 shows 6-fold rotational symmetry. In contrast, in the cubic crystal form at 2.55 A resolution described here RepA has 3-fold symmetry and consists of a trimer of dimers. To study structure-function relationships, a series of repA deletion mutants and mutations yielding single amino...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Alanine
Share to Catalytic Domain

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

Share to Crystallography, X-Ray

Share to Dimerization

Share to DNA Helicases

Share to DNA Replication

Share to Glutamine

Source

Open in PubMed Open full text

Identifiers

PMID: 14530440
DOI: 10.1093/nar/gkg790
PMCID: PMC219471

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

Hexameric RSF1010 helicase RepA: the structural and functional importance of single amino acid residues.PMID 14530440Read ↗

Residues within the B' motif are critical for DNA binding by the superfamily 3 helicase Rep40 of adeno-associated virus type 2.Semantic proximity Read ↗

Replication Protein A, the Main Eukaryotic Single-Stranded DNA Binding Protein, a Focal Point in Cellular DNA MetabolismSemantic proximity Read ↗

Structural changes in RepA, a plasmid replication initiator, upon binding to origin DNA.Semantic proximity Read ↗

Identification of a Functionally Relevant Adeno-Associated Virus Rep68 Oligomeric Interface.Semantic proximity Read ↗

DNA Helicase Activity Is Associated with the Replication Initiator Protein Rep of Tomato Yellow Leaf Curl GeminivirusSemantic proximity Read ↗

REPercussions: how geminiviruses recruit host factors for replicationSemantic proximity Read ↗

Plasmid P1 RepA is homologous to the F plasmid RepE class of initiators.Semantic proximity Read ↗

Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA.Semantic proximity Read ↗

5'-Single-stranded/duplex DNA junctions are loading sites for E. coli UvrD translocase.Semantic proximity Read ↗

DNA-binding orientation and domain conformation of the E. coli rep helicase monomer bound to a partial duplex junction: single-molecule studies of fluorescently labeled enzymes.Semantic proximity Read ↗

Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus.Semantic proximity Read ↗

The Rep52 gene product of adeno-associated virus is a DNA helicase with 3'-to-5' polarity.Semantic proximity Read ↗

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