8hoy: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q5IXW8_MONPV Q5IXW8_MONPV]  
[https://www.uniprot.org/uniprot/DPOL_MONPV DPOL_MONPV] Catalyzes DNA synthesis. Acquires processivity by associating with a heterodimeric processivity factor comprised of the viral OPG148 and OPG116 proteins, thereby forming the DNA polymerase holoenzyme. Displays 3'- to 5' exonuclease activity. Might participate in viral DNA recombination. Does not perform OPG116/D4synthesis across an abasic site.[UniProtKB:P06856]
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</StructureSection>
</StructureSection>

Latest revision as of 08:02, 18 September 2024

Cryo-EM structure of monkeypox virus DNA replication holoenzyme F8, A22 and E4 complex without DNA at 2.76 angostramCryo-EM structure of monkeypox virus DNA replication holoenzyme F8, A22 and E4 complex without DNA at 2.76 angostram

Structural highlights

8hoy is a 3 chain structure with sequence from Monkeypox virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.76Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPOL_MONPV Catalyzes DNA synthesis. Acquires processivity by associating with a heterodimeric processivity factor comprised of the viral OPG148 and OPG116 proteins, thereby forming the DNA polymerase holoenzyme. Displays 3'- to 5' exonuclease activity. Might participate in viral DNA recombination. Does not perform OPG116/D4synthesis across an abasic site.[UniProtKB:P06856]

8hoy, resolution 2.76Å

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OCA
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