5n2g
From Proteopedia
Structure of the E9 DNA polymerase from vaccinia virus in complex with manganese
Structural highlights
FunctionDPOL_VACCC Catalyzes DNA synthesis. Acquires processivity by associating with a heterodimeric processivity factor comprised of the viral A20 and D4 proteins, thereby forming the DNA polymerase holoenzyme. Displays 3'- to 5' exonuclease activity. Might participate in viral DNA recombination. Does not perform translesion synthesis across an abasic site (By similarity). Publication Abstract from PubMedVaccinia virus (VACV), the prototype member of the Poxviridae, replicates in the cytoplasm of an infected cell. The catalytic subunit of the DNA polymerase E9 binds the heterodimeric processivity factor A20/D4 to form the functional polymerase holoenzyme. Here we present the crystal structure of full-length E9 at 2.7 A resolution that permits identification of important poxvirus-specific structural insertions. One insertion in the palm domain interacts with C-terminal residues of A20 and thus serves as the processivity factor-binding site. This is in strong contrast to all other family B polymerases that bind their co-factors at the C terminus of the thumb domain. The VACV E9 structure also permits rationalization of polymerase inhibitor resistance mutations when compared with the closely related eukaryotic polymerase delta-DNA complex. The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.,Tarbouriech N, Ducournau C, Hutin S, Mas PJ, Man P, Forest E, Hart DJ, Peyrefitte CN, Burmeister WP, Iseni F Nat Commun. 2017 Nov 13;8(1):1455. doi: 10.1038/s41467-017-01542-z. PMID:29129932[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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