3bn0

The ribosomal protein S16 from Aquifex aeolicus

spinqualitylabelsall models 3bn0, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3bn0 is a 1 chain structure with sequence from "aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Related: 1emw Gene: rpsP ("Aquifex aeolicus" Huber and Stetter 2001) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Understanding the mechanisms that dictate protein stability is of large relevance, for instance, to enable design of temperature-tolerant enzymes with high enzymatic activity over a broad temperature interval. In an effort to identify such mechanisms, we have performed a detailed comparative study of the folding thermodynamics and kinetics of the ribosomal protein S16 isolated from a mesophilic (S16(meso)) and hyperthermophilic (S16(thermo)) bacterium by using a variety of biophysical methods. As basis for the study, the 2.0 A X-ray structure of S16(thermo) was solved using single wavelength anomalous dispersion phasing. Thermal unfolding experiments yielded midpoints of 59 and 111 degrees C with associated changes in heat capacity upon unfolding (DeltaC(p)(0)) of 6.4 and 3.3 kJ mol(-1) K(-1), respectively. A strong linear correlation between DeltaC(p)(0) and melting temperature (T(m)) was observed for the wild-type proteins and mutated variants, suggesting that these variables are intimately connected. Stopped-flow fluorescence spectroscopy shows that S16(meso) folds through an apparent two-state model, whereas S16(thermo) folds through a more complex mechanism with a marked curvature in the refolding limb indicating the presence of a folding intermediate. Time-resolved energy transfer between Trp and N-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-yl)methyl iodoacetamide of proteins mutated at selected positions shows that the denatured state ensemble of S16(thermo) is more compact relative to S16(meso). Taken together, our results suggest the presence of residual structure in the denatured state ensemble of S16(thermo) that appears to account for the large difference in quantified DeltaC(p)(0) values and, in turn, parts of the observed extreme thermal stability of S16(thermo). These observations may be of general importance in the design of robust enzymes that are highly active over a wide temperature span. Extreme temperature tolerance of a hyperthermophilic protein coupled to residual structure in the unfolded state.,Wallgren M, Aden J, Pylypenko O, Mikaelsson T, Johansson LB, Rak A, Wolf-Watz M J Mol Biol. 2008 Jun 13;379(4):845-58. Epub 2008 Apr 8. PMID:18471828 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein S16

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