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

Evidence for functional significance of the permuted C motif in Co2+-stimulated RNA-dependent RNA polymerase of infectious bursal disease virus.

The Journal of general virology - 1 Oct 2007

Letzel Tobias, Mundt Egbert, Gorbalenya Alexander E

Abstract excerpt

Segment B of bisegmented infectious bursal disease virus (IBDV) encodes virus protein 1 (VP1), possessing RNA-dependent RNA polymerase (RdRp) activity. This multidomain protein includes an RdRp domain with a non-canonical order of three sequence motifs forming the active site: C-A-B. The A-B-C order of the motifs, as found in RdRps of the majority of viruses, was converted by relocation (permutation) of motif C...

Read the complete abstract on PubMed

Topics

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

Share to Cobalt
Share to Cricetinae
Share to Infectious bursal disease virus

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

Share to Kidney

Share to Peptide Fragments

Share to Recombination, Genetic

Share to RNA-Dependent RNA Polymerase

Share to Viral Proteins

Source

Identifiers

PMID: 17872536
DOI: 10.1099/vir.0.82890-0

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

Evidence for functional significance of the permuted C motif in Co2+-stimulated RNA-dependent RNA polymerase of infectious bursal disease virus.PMID 17872536Read ↗

A cysteine-rich motif in poliovirus protein 2C(ATPase) is involved in RNA replication and binds zinc in vitro.Semantic proximity Read ↗

Retroviral nucleocapsid protein-metal ion interactions: folding and sequence variants.Semantic proximity Read ↗

Clustered Lysine Residues of the Canine Distemper Virus Matrix Protein Regulate Membrane Association and Budding Activity.Semantic proximity Read ↗

Manganese-dependent polioviruses caused by mutations within the viral polymerase.Semantic proximity Read ↗

Structural features stabilized by divalent cation coordination within hepatitis E virus ORF1 are critical for viral replicationSemantic proximity Read ↗

ø29 DNA polymerase residue Lys383, invariant at motif B of DNA-dependent polymerases, is involved in dNTP binding.Semantic proximity Read ↗

VP1 of infectious bursal disease virus is an RNA-dependent RNA polymeraseSemantic proximity Read ↗

The 2.6-Angstrom Structure of Infectious Bursal Disease Virus-Derived T=1 Particles Reveals New Stabilizing Elements of the Virus CapsidSemantic proximity Read ↗

Structural explanation for the role of Mn2+ in the activity of phi6 RNA-dependent RNA polymerase.Semantic proximity Read ↗

Structure and function of virion RNA polymerase of crAss-like phageSemantic proximity Read ↗

Mapping the triphosphatase active site of baculovirus mRNA capping enzyme LEF4 and evidence for a two-metal mechanism.Semantic proximity Read ↗

Foot-and-mouth disease virus 2C is a hexameric AAA+ protein with a coordinated ATP hydrolysis mechanism.Semantic proximity Read ↗

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