4ZG5

Structural and functional insights into Survival endonuclease, an important virulence factor of Brucella abortus

Replaces:  4QEA

Summary for 4ZG5

• Entry DOI: 10.2210/pdb4zg5/pdb
• Descriptor: 5'-nucleotidase SurE, MAGNESIUM ION (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Brucella abortus S19
• Cellular location: Cytoplasm : B2S5B9
• Total number of polymer chains: 4
• Total formula weight: 114555.20

Authors

Tarique, K.F.,Abdul Rehman, S.A.,Devi, S.,Gourinath, S. (deposition date: 2015-04-22, release date: 2015-05-06, Last modification date: 2023-11-08)

Primary citation

Tarique, K.F.,Abdul Rehman, S.A.,Devi, S.,Tomar, P.,Gourinath, S.
Structural and functional insights into the stationary-phase survival protein SurE, an important virulence factor of Brucella abortus
Acta Crystallogr.,Sect.F, 72:386-396, 2016

PubMed Abstract: 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 Å. 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 α + β fold, and a C-terminal domain that belongs to the α/β 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.

PubMed: 27139831
DOI: 10.1107/S2053230X16005999

Experimental method

X-RAY DIFFRACTION (1.9 Å)