Abstract 1870 Crystal structure and ligand-binding specificity of the Borrelia burgdorferi proteins BmpA and BmpB
Borrelia burgdorferi is a diderm bacterium and the causative agent of Lyme disease. Studies have shown that proteins BmpA and BmpB bind to laminin, a key component of the host's extracellular matrix. However, previous research identified a paralogous protein, BmpD, as a nucleoside-binding protein. This raises the question of whether BmpA and BmpB also share this nucleoside-binding function or exclusively bind laminin. To elucidate the structure and function of BmpA, we determined its crystal structure at a resolution of 2.90 Å.
Authors
- Qian Liu (ORCID: https://orcid.org/0000-0002-8398-1021)
- Daniel Fernández (ORCID: https://orcid.org/0000-0002-6221-152X)
- Naima G. Sharaf (ORCID: https://orcid.org/0000-0002-3662-9228)
Institutions
- Stanford University (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109939
- Primary Topic
- Insect and Pesticide Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Institutes of Health