Open AccessStructure of Rv1848 (UreA), the Mycobacterium tuberculosis urease γ subunit
Author(s) -
Habel Jeff E.,
Bursey Evan H.,
Rho BeomSeop,
Kim ChangYub,
Segelke Brent W.,
Rupp Bernhard,
Park Min S.,
Terwilliger Thomas C.,
Hung LiWei
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110019536
Subject(s) - urease , mycobacterium tuberculosis , protein subunit , urea , microbiology and biotechnology , chemistry , tuberculosis , biochemistry , biology , medicine , pathology , gene
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.