6H24
X-Ray Crystal Structure of the MSBI1.176 WH1 Domain, a Replication Protein Isolated from a Multiple Sclerosis Patient
Summary for 6H24
Entry DOI | 10.2210/pdb6h24/pdb |
Descriptor | Replication protein (2 entities in total) |
Functional Keywords | repa, msbi1.176, wh1, sclerosis, replication |
Biological source | Sphinx1.76-related DNA |
Total number of polymer chains | 2 |
Total formula weight | 30908.88 |
Authors | Kilic, T.,Popov, A.N.,Hansman, G.S. (deposition date: 2018-07-13, release date: 2019-05-15, Last modification date: 2024-05-15) |
Primary citation | Kilic, T.,Popov, A.N.,Burk-Korner, A.,Koromyslova, A.,Zur Hausen, H.,Bund, T.,Hansman, G.S. Structural analysis of a replication protein encoded by a plasmid isolated from a multiple sclerosis patient. Acta Crystallogr D Struct Biol, 75:498-504, 2019 Cited by PubMed 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. PubMed: 31063152DOI: 10.1107/S2059798319003991 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.53 Å) |
Structure validation
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