3zzp

Circular permutant of ribosomal protein S6, lacking edge strand beta- 2 of wild-type S6.

spinqualitylabelsall models 3zzp, resolution 0.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zzp is a 1 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1qjh, 1cqn, 2bvz, 1twt, 1cqm, 1lou, 2bxj, 1ris, 1l1u Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RS6_THETH] Located on the outer edge of the platform on the body of the 30S subunit (By similarity). Publication Abstract from PubMed Folding of the ribosomal protein S6 is a malleable process controlled by two competing, and partly overlapping, folding nuclei. Together, these nuclei extend over most of the S6 structure, except the edge strand beta2, which is consistently missing in the folding transition states; despite being part of the S6 four-stranded sheet, beta2 seems not to be part of the cooperative unit of the protein. The question is then whether beta2 can be removed from the S6 structure without compromising folding cooperativity or native state integrity. To investigate this, we constructed a truncated variant of S6 lacking beta2, reducing the size of the protein from 96 to 76 residues (S6(Deltabeta2)). The new S6 variant expresses well in Escherichia coli and has a well dispersed heteronuclear single quantum correlation spectrum and a perfectly wild-type-like crystal structure, but with a smaller three-stranded beta-sheet. Moreover, S6(Deltabeta2) displays an archetypical v-shaped chevron plot with decreased slope of the unfolding limb, as expected from a protein with maintained folding cooperativity and reduced size. The results support the notion that foldons, as defined by the structural distribution of the folding nuclei, represent a property-based level of hierarchy in the build-up of larger protein structures and suggest that the role of beta2 in S6 is mainly in intermolecular binding, consistent with the position of this strand in the ribosomal assembly. Trimming down a protein structure to its bare foldons: spatial organization of the cooperative unit.,Haglund E, Danielsson J, Kadhirvel S, Lindberg MO, Logan DT, Oliveberg M J Biol Chem. 2012 Jan 20;287(4):2731-8. Epub 2011 Nov 22. PMID:22117065 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein S6

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