1. Structure of Rv1848 (UreA), theMycobacterium tuberculosisurease γ subunit
- Author
-
Bernhard Rupp, Min S. Park, Evan H. Bursey, Li-Wei Hung, Beom Seop Rho, Chang Yub Kim, Brent W. Segelke, Jeff E. Habel, and Thomas C. Terwilliger
- Subjects
Models, Molecular ,Urease ,Protein subunit ,Molecular Sequence Data ,Biophysics ,chemical and pharmacologic phenomena ,Biology ,Crystallography, X-Ray ,Enterobacter aerogenes ,Biochemistry ,Mycobacterium tuberculosis ,chemistry.chemical_compound ,Protein structure ,Structural Biology ,Genetics ,Structural Communications ,Amino Acid Sequence ,Protein Structure, Quaternary ,chemistry.chemical_classification ,Sequence Homology, Amino Acid ,respiratory system ,bacterial infections and mycoses ,Condensed Matter Physics ,biology.organism_classification ,Protein Structure, Tertiary ,Amino acid ,Protein Subunits ,chemistry ,Urea ,biology.protein ,Protein quaternary structure ,Sequence Alignment - Abstract
The crystal structure of the urease gamma subunit (UreA) from Mycobacterium tuberculosis, Rv1848, has been determined at 1.8 A 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 (alphabetagamma)(3) composition observed for other bacterial ureases. The gamma subunit may be of primary importance for the formation of the urease quaternary structure.
- Published
- 2010
- Full Text
- View/download PDF