Structure of NMB1585, a Regulator from Neisseria meningitidis
Author Information
Author(s): Nichols Charles E., Sainsbury Sarah, Ren Jingshan, Walter Thomas S., Verma Anil, Stammers David K., Saunders Nigel J., Owens Raymond J.
Primary Institution: University of Oxford
Hypothesis
The study aims to elucidate the structure and function of the MarR-family regulator NMB1585 from Neisseria meningitidis.
Conclusion
The crystal structure of NMB1585 was solved at 2.1 Å resolution, revealing its dimeric form and potential for DNA binding.
Supporting Evidence
- NMB1585 was shown to bind to its own promoter region in a gel-shift assay.
- The structure of NMB1585 resembles other MarR proteins, indicating a conserved mechanism of action.
- NMB1585 is pre-configured for DNA binding, suggesting its role as a transcriptional repressor.
Takeaway
Scientists figured out the shape of a protein called NMB1585, which helps bacteria control their genes. This protein can stick to DNA and might help the bacteria resist drugs.
Methodology
The structure was determined using multiwavelength anomalous dispersion methods with selenomethionine-labeled crystals.
Limitations
The physiological role of NMB1585 and its natural ligands remain unknown.
Digital Object Identifier (DOI)
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