- UreG, a chaperone in the urease assembly process, is an intrinsically unstructured GTPase that specifically binds Zn
- Structural basis for the molecular properties of cytochrome c(6)
- Molecular characterization of Bacillus pasteurii UreE, a metal-binding chaperone for the assembly of the urease active site.
- Structural basis for Ni2+ transport and assembly of the urease active site by the metallochaperone UreE from Bacillus pasteurii.
- Crystal structure of oxidized Bacillus pasteurii cytochrome c(553) at 0.97-angstrom resolution.
Cytochrome c-553 from the alkalophilic bacterium Bacillus pasteurii has the primary structure characteristics of a lipoprotein.
1999) BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. 264(2). p.380-387 Mark(
- The primary structure of Rhodoferax fermentans high-potential iron-sulfur protein, an electron donor to the photosynthetic reaction center