Solution NMR structure of the 30S ribosomal protein S28E from <i>Pyrococcus horikoshii</i>

Abstract

Abstract We report NMR assignments and solution structure of the 71‐residue 30S ribosomal protein S28E from the archaean Pyrococcus horikoshii , target JR19 of the Northeast Structural Genomics Consortium. The structure, determined rapidly with the aid of automated backbone resonance assignment (AutoAssign) and automated structure determination (AutoStructure) software, is characterized by a four‐stranded β‐sheet with a classic Greek‐key topology and an oligonucleotide/oligosaccharide β‐barrel (OB) fold. The electrostatic surface of S28E exhibits positive and negative patches on opposite sides, the former constituting a putative binding site for RNA. The 13 C‐terminal residues of the protein contain a consensus sequence motif constituting the signature of the S28E protein family. Surprisingly, this C‐terminal segment is unstructured in solution.