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Article

Crystal structure of epstein-barr virus DNA polymerase processivity factor BMRF1.

The Journal of biological chemistry - 18 Dec 2009

Murayama Kazutaka, Nakayama Sanae, Kato-Murayama Miyuki, Akasaka Ryogo, Ohbayashi Naomi, Kamewari-Hayami Yuki, Terada Takaho, Shirouzu Mikako, Tsurumi Tatsuya, Yokoyama Shigeyuki

Abstract excerpt

The DNA polymerase processivity factor of the Epstein-Barr virus, BMRF1, associates with the polymerase catalytic subunit, BALF5, to enhance the polymerase processivity and exonuclease activities of the holoenzyme. In this study, the crystal structure of C-terminally truncated BMRF1 (BMRF1-DeltaC...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19801550
DOI: 10.1074/jbc.M109.051581
PMCID: PMC2791018

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19801550-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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