2lkv

Staphylococcal Nuclease PHS variant

spinqualitylabelsall models 2lkv, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lkv is a 1 chain structure with sequence from Staphylococcus aureus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: nuc, MW0769 (Staphylococcus aureus) Activity: Micrococcal nuclease, with EC number 3.1.31.1 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Mannosylglycerate is a compatible solute typical of thermophilic marine microorganisms that has a remarkable ability to protect proteins from thermal denaturation. This ionic solute appears to be a universal stabilizing agent, but the extent of protection depends on the specific protein examined. To understand how mannosylglycerate confers protection, we have been studying its influence on the internal motions of a hyperstable staphylococcal nuclease (SNase). Previously, we found a correlation between the magnitude of protein stabilization and the restriction of fast backbone motions. We now report the effect of mannosylglycerate on the fast motions of side-chains and on the slower unfolding motions of the protein. Side-chain motions were assessed by (13) CH(3) relaxation measurements and model-free analysis while slower unfolding motions were probed by H/D exchange measurements at increasing concentrations of urea. Side-chain motions were little affected by the presence of different concentrations of mannosylglycerate or even by the presence of urea (0.25M), and show no correlation with changes in the thermodynamic stability of SNase. Native hydrogen exchange experiments showed that, contrary to reports on other stabilizing solutes, mannosylglycerate restricts local motions in addition to the global motions of the protein. The protein unfolding/folding pathway remained undisturbed in the presence of mannosylglycerate but the solute showed a specific effect on the local motions of beta-sheet residues. This work reinforces the link between solute-induced stabilization and restriction of protein motions at different timescales, and shows that the solute preferentially affects specific structural elements of SNase. Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow beta-sheet motions.,Pais TM, Lamosa P, Matzapetakis M, Turner DL, Santos H Protein Sci. 2012 Aug;21(8):1126-37. doi: 10.1002/pro.2100. Epub 2012 Jun 15. PMID:22619184 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Staphylococcal nuclease

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