2kjv

Solution structure and backbone dynamics of the ribosomal protein S6wt

spinqualitylabelsall models 2kjv Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kjv is a 1 chain structure with sequence from Thermus thermophilus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RS6_THET8 Located on the outer edge of the platform on the body of the 30S subunit.[HAMAP-Rule:MF_00360] 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 The ribosomal protein S6 from Thermus thermophilus has served as a model system for the study of protein folding, especially for understanding the effects of circular permutations of secondary structure elements. This study presents the structure of a permutant protein, the 96-residue P(54-55), and the structure of its 101-residue parent protein S6(wt) in solution. The data also characterizes the effects of circular permutation on the backbone dynamics of S6. Consistent with crystallographic data on S6(wt), the overall solution structures of both P(54-55) and S6(wt) show a beta-sheet of four antiparallel beta-strands with two alpha-helices packed on one side of the sheet. In clear contrast to the crystal data, however, the solution structure of S6(wt) reveals a disordered loop in the region between beta-strands 2 and 3 (Leu43-Phe60) instead of a well-ordered stretch and associated hydrophobic mini-core observed in the crystal structure. Moreover, the data for P(54-55) show that the joined wild-type N- and C-terminals form a dynamically robust stretch with a hairpin structure that complies with the in silico design. Taken together, the results explain why the loop region of the S6(wt) structure is relatively insensitive to mutational perturbations, and why P(54-55) is more stable than S6(wt): the permutant incision at Lys54-Asp55 is energetically neutral by being located in an already disordered loop whereas the new hairpin between the wild-type N- and C-termini is stabilizing. Solution structures and backbone dynamics of the ribosomal protein S6 and its permutant P(54-55).,Ohman A, Oman T, Oliveberg M Protein Sci. 2010 Jan;19(1):183-9. PMID:19937661 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein S6

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