Structure of Rv1848 (UreA), the Mycobacterium tuberculosis urease γ subunit

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-07, Vol.66 (7), p.781-786
• Main Authors: Habel, Jeff E., Bursey, Evan H., Rho, Beom-Seop, Kim, Chang-Yub, Segelke, Brent W., Rupp, Bernhard, Park, Min S., Terwilliger, Thomas C., Hung, Li-Wei
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Crystallography, X-Ray; Models, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis; Mycobacterium tuberculosis - enzymology; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits - chemistry; Sequence Alignment; Sequence Homology, Amino Acid; Structural Communications; structural genomics; urease; Urease - chemistry
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309110019536

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.