TAILIEUCHUNG - Báo cáo khoa học: Structural and functional studies on a mesophilic stationary phase survival protein (Sur E) from Salmonella typhimurium

SurE, the stationary-phase survival protein of Salmonella typhimurium, forms part of a stress survival operon regulated by the stationary-phase RNA polymerase alternative sigma factor. SurE is known to improve bacterial viability during stress conditions. | ỊFEBS Journal Structural and functional studies on a mesophilic stationary phase survival protein Sur E from Salmonella typhimurium A. Pappachan1 H. S. Savithri2 and M. R. N. Murthy1 1 Molecular Biophysics Unit Indian Institute of Science Bangalore India 2 Department of Biochemistry Indian Institute of Science Bangalore India Keywords divalent metal ion domain swapping mononucleotidase stationary phase Sur E Correspondence M. R. N. Murthy Molecular Biophysics Unit Indian Institute of Science Bangalore- 560 012 India Fax 91 80 23600535 Tel 91 80 22932458 E-mail mrn@ Database The coordinates and structure factors of the crystal structures described in this study have been submitted to the Protein Data Bank and the structures have been assigned the accession codes 2v4n and 2v4o for the F222 SurE structure and the C2 SurE structure respectively Received 13 August 2008 revised 24 September 2008 accepted 26 September 2008 doi SurE the stationary-phase survival protein of Salmonella typhimurium forms part of a stress survival operon regulated by the stationary-phase RNA polymerase alternative sigma factor. SurE is known to improve bacterial viability during stress conditions. It functions as a phosphatase specific to nucleoside monophosphates. In the present study we reported the X-ray crystal structure of SurE from Salmonella typhimurium. The protein crystallized in two forms orthorhombic F222 and monoclinic C2. The two structures were determined to resolutions of and A respectively. The protein exists as a domain-swapped dimer. The residue D230 is involved in several interactions that are probably crucial for domain swapping. A divalent metal ion is found at the active site of the enzyme which is consistent with the divalent metal ion-dependent activity of the enzyme. Interactions of the conserved DD motif present at the N-terminus with the phosphate and the Mg2 present in the active site suggest that these .

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