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Structural analysis of a replication protein encoded by a plasmid isolated from a multiple sclerosis patient
Author(s) -
Kilic Turgay,
Popov Alexander N.,
Burk-Körner Amelie,
Koromyslova Anna,
zur Hausen Harald,
Bund Timo,
Hansman Grant S.
Publication year - 2019
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798319003991
Subject(s) - encode , biology , plasmid , computational biology , genetics , dna , gene
Bovine meat and milk factors (BMMFs) are circular, single‐stranded episomal DNAs that have been detected in bovine meat and milk products. BMMFs are thought to have roles in human malignant and degenerative diseases. BMMFs encode a replication initiator protein (Rep) that is actively transcribed and translated in human cells. In this study, a Rep WH1 domain encoded on a BMMF (MSBI1.176) isolated from a multiple sclerosis human brain sample was determined to 1.53 Å resolution using X‐ray crystallography. The overall structure of the MSBI1.176 WH1 domain was remarkably similar to other Rep structures, despite having a low (28%) amino‐acid sequence identity. The MSBI1.176 WH1 domain contained elements common to other Reps, including five α‐helices, five β‐strands and a hydrophobic pocket. These new findings suggest that the MSBI1.176 Rep might have comparable roles and functions to other known Reps of different origins.