4zg5

Publication Abstract from PubMed

The stationary-phase survival protein SurE from Brucella abortus (BaSurE) is a metal-dependent phosphatase that is essential for the survival of this bacterium in the stationary phase of its life cycle. Here, BaSurE has been biochemically characterized and its crystal structure has been determined to a resolution of 1.9 A. BaSurE was found to be a robust enzyme, showing activity over wide ranges of temperature and pH and with various phosphoester substrates. The active biomolecule is a tetramer and each monomer was found to consist of two domains: an N-terminal domain, which forms an approximate alpha + beta fold, and a C-terminal domain that belongs to the alpha/beta class. The active site lies at the junction of these two domains and was identified by the presence of conserved negatively charged residues and a bound Mg(2+) ion. Comparisons of BaSurE with its homologues have revealed both common features and differences in this class of enzymes. The number and arrangement of some of the equivalent secondary structures, which are seen to differ between BaSurE and its homologues, are responsible for a difference in the size of the active-site area and the overall oligomeric state of this enzyme in other organisms. As it is absent in mammals, it has the potential to be a drug target.

Structural and functional insights into the stationary-phase survival protein SurE, an important virulence factor of Brucella abortus.,Tarique KF, Abdul Rehman SA, Devi S, Tomar P, Gourinath S Acta Crystallogr F Struct Biol Commun. 2016 May 1;72(Pt 5):386-96. doi:, 10.1107/S2053230X16005999. Epub 2016 Apr 22. PMID:27139831^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.