1m5q | pdb_00001m5q

Crystal structure of a novel Sm-like archaeal protein from Pyrobaculum aerophilum

spinqualitylabelsall models 1m5q, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1m5q is a 28 chain structure with sequence from Atcc 51768. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACY, CD, GOL, NA NonStd Res: MSE Related: 1i8f, 1jbm, 1i4k, 1d3b Gene: SmAP3 gene (Pae2122) (ATCC 51768) 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 To better understand the roles of Sm proteins in forming the cores of many RNA-processing ribonucleoproteins, we determined the crystal structure of an atypical Sm-like archaeal protein (SmAP3) in which the conserved Sm domain is augmented by a previously uncharacterized, mixed alpha/beta C-terminal domain. The structure reveals an unexpected SmAP3 14-mer that is perforated by a cylindrical pore and is bound to 14 cadmium (Cd(2+)) ions. Individual heptamers adopt either "apical" or "equatorial" conformations that chelate Cd(2+) differently. SmAP3 forms supraheptameric oligomers (SmAP3)(n = 7,14,28) in solution, and assembly of the asymmetric 14-mer is modulated by differential divalent cation-binding in apical and equatorial subunits. Phylogenetic and sequence analyses substantiate SmAP3s as a unique subset of SmAPs. These results distinguish SmAP3s from other Sm proteins and provide a model for the structure and properties of Sm proteins >100 residues in length, e.g., several human Sm proteins. Structure and assembly of an augmented Sm-like archaeal protein 14-mer.,Mura C, Phillips M, Kozhukhovsky A, Eisenberg D Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4539-44. Epub 2003 Mar 31. PMID:12668760 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sm-like protein

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