1v8q | pdb_00001v8q

Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8

spinqualitylabelsall models 1v8q, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1v8q is a 4 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. Ligands: DTT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN Function [RL27_THET8] Found on the solvent side of the large subunit.[HAMAP-Rule:MF_00539] 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 Ribosomal protein L27 is located near the peptidyltransferase center at the interface of ribosomal subunits, and is important for ribosomal assembly and function. We report the crystal structure of ribosomal protein L27 from Thermus thermophilus HB8, which was determined by the multiwavelength anomalous dispersion method and refined to an R-factor of 19.7% (R(free) = 23.6%) at 2.8 A resolution. The overall fold is an all beta-sheet hybrid. It consists of two sets of four-stranded beta-sheets formed around a well-defined hydrophobic core, with a highly positive charge on the protein surface. The structure of ribosomal protein L27 from T. thermophilus HB8 in the RNA-free form is investigated, and its functional roles in the ribosomal subunit are discussed. Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8.,Wang H, Takemoto CH, Murayama K, Sakai H, Tatsuguchi A, Terada T, Shirouzu M, Kuramitsu S, Yokoyama S Protein Sci. 2004 Oct;13(10):2806-10. Epub 2004 Aug 31. PMID:15340170 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein L27

Proteopedia Page Contributors and Editors (what is this?)

OCA