Structural analysis of a replication protein encoded by a plasmid isolated from a multiple sclerosis patient
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Author(s)
Popov, Alexander N
Burk-Koerner, Amelie
Koromyslova, Anna
zur Hausen, Harald
Bund, Timo
Hansman, Grant S
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Abstract
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.
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Acta Crystallographica Section D
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75
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5
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Structural biology (incl. macromolecular modelling)
Science & Technology
Life Sciences & Biomedicine
Physical Sciences
Biochemical Research Methods
Biochemistry & Molecular Biology
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Kilic, T; Popov, AN; Burk-Koerner, A; Koromyslova, A; zur Hausen, H; Bund, T; Hansman, GS, Structural analysis of a replication protein encoded by a plasmid isolated from a multiple sclerosis patient, Acta Crystallographica Section D, 2019, 75 (5), pp. 498-504