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Literature summary for 2.7.7.48 extracted from

  • Shu, B.; Gong, P.
    Structural basis of viral RNA-dependent RNA polymerase catalysis and translocation (2016), Proc. Natl. Acad. Sci. USA, 113, E4005-E4014.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in complex with NTP substrate, X-ray diffraction structure determination and analysis at 2.45-2.78 A resolution, analysis of multiple nucleotide-incorporation events and different NAC states Enterovirus A71

Organism

Organism UniProt Comment Textmining
Enterovirus A71
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Enterovirus C
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information viral RdRP elongation nucleotide addition cycle (NAC), structure-function analysis, overview Enterovirus A71 ?
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 ?

Synonyms

Synonyms Comment Organism
RDRP
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 Enterovirus C
RDRP
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 Enterovirus A71

General Information

General Information Comment Organism
additional information seven RdRP elongation complex structures derived from a crystal lattice that allows three RdRP nucleotide addition cycle (NAC) events. NTP recognition and translocation mechanisms in viral RdRPs and uniqueness of the viral RdRPs compared with other processive polymerases, modelling, overview. Determination of initial NTP binding, active site closure, and, in particular the RNA motion during translocation that shows an asymmetric movement of the two strands in the template-product duplex Enterovirus A71
additional information several structural states of the poliovirus RdRP nucleotide addition cycle (NAC) reveal a unique palm domain-based active site closure mechanism and propose a six-state NAC model including a hypothetical state representing translocation intermediates. NTP recognition and translocation mechanisms in viral RdRPs and uniqueness of the viral RdRPs compared with other processive polymerases, modelling, overview Enterovirus C
physiological function viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription Enterovirus C
physiological function viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription Enterovirus A71