Download citation
Download citation
link to html
The crystal structure of the urease γ subunit (UreA) from Mycobacterium tuberculosis, Rv1848, has been determined at 1.8 Å resolution. The asymmetric unit contains three copies of Rv1848 arranged into a homotrimer that is similar to the UreA trimer in the structure of urease from Klebsiella aerogenes. Small-angle X-ray scattering experiments indicate that the Rv1848 protein also forms trimers in solution. The observed homotrimer and the organization of urease genes within the M. tuberculosis genome suggest that M. tuberculosis urease has the (αβγ)3 composition observed for other bacterial ureases. The γ subunit may be of primary importance for the formation of the urease quaternary structure.

Supporting information

pdf

Portable Document Format (PDF) file https://doi.org/10.1107/S1744309110019536/gx5165sup1.pdf
SAXS experimental data.

pdf

Portable Document Format (PDF) file https://doi.org/10.1107/S1744309110019536/gx5165sup2.pdf
Statistics from the Porod and P(r) graph calculations.

PDB reference: Rv1848, 2fvh


Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds