2m00 | pdb_00002m00

Solution structure of staphylococcal nuclease E43S mutant in the presence of ssDNA and Cd2+

spinqualitylabelsall models 2m00, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2m00 is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus mw2. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: nuc, MW0769 (Staphylococcus aureus subsp. aureus MW2) Activity: Micrococcal nuclease, with EC number 3.1.31.1 Resources: FirstGlance, OCA, RCSB, PDBsum Function [NUC_STAAW] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond (By similarity). Publication Abstract from PubMed Staphylococcal nuclease (SNase) catalyzes the hydrolysis of the phosphate backbone of DNA and RNA leaving 3'-phosphate mononucleotides and dinucleotides. SNase has been extensively used as a model protein for investigating enzymatic mechanism, thermodynamic stability, and protein folding. An unanswered question regarding enzymatic structure-function relationship is how SNase is capable of binding DNA and catalyzing the DNA hydrolysis. For understanding the mechanism of SNase-DNA interaction at the structural level, we have investigated the interactions between the E43S-mutant SNase ([E43S]SNase) and ssDNA in the presence of Cd(2+) using various NMR techniques including pulsed field gradient diffusion measurement, NMR titration and affinity measurement, chemical shift mapping, backbone dynamics, and three dimensional structural determination. [E43S]SNase retains the similar DNA-binding ability to the native SNase but loses its catalytic activity, and binding of ssDNA/Cd(2+) to [E43S]SNase induced certain degree backbone conformational exchange motion in the ssDNA and Cd(2+) binding regions, which might account for the preferential binding of DNA. Based on the NMR-derived structure of ssDNA/Cd(2+)-bound [E43S]SNase, we have built a three-dimensional model of the [E43S]SNase-ssDNA-Cd(2+) complex. The resulting model enabled the functional roles of SNase to be discussed, in particular the action of nuclease on ssDNA. Modeling of the [E43S]SNase-ssDNA-Cd(2+) complex: Structural insight into the action of nuclease on ssDNA.,Xie T, Feng Y, Shan L, Wang J Arch Biochem Biophys. 2013 Feb 14. pii: S0003-9861(13)00038-6. doi:, 10.1016/j.abb.2013.02.003. PMID:23416741 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Staphylococcal nuclease

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