Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 66, Issue -, Pages 1657-1661Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309110042958
Keywords
BfrB; Mycobacterium tuberculosis; ferritins
Funding
- National Institutes of Health [AI068135]
- Colorado State University (NIH NIAID) [NO1 AI-75320]
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Mycobacterium tuberculosis (Mtb) is the causative agent of the deadly disease tuberculosis. Iron acquisition, regulation and storage are critical for the survival of this pathogen within a host. Thus, understanding the mechanisms of iron metabolism in Mtb will shed light on its pathogenic nature, as iron is important for infection. Ferritins are a superfamily of protein nanocages that function in both iron detoxification and storage, and Mtb contains both a predicted ferritin and a bacterioferritin. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the ferritin homolog (Mtb BfrB, Rv3841) is reported. An Mtb BfrB crystal grown at pH 6.5 using the hanging-drop vapor-diffusion technique diffracted to 2.50 A resolution and belonged to space group C2, with unit-cell parameters a = 226.2, b = 226.8, c = 113.7 A, beta = 94.7 degrees and with 24 subunits per asymmetric unit. Furthermore, modeling the crystal structure of a homologous ferritin into a low-resolution small-angle X-ray scattering (SAXS) electron-density envelope is consistent with the presence of 24 subunits in the BfrB protein cage quaternary structure.
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