Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.

TitleSolution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Publication TypeJournal Article
Year of Publication2003
AuthorsAramini, JM, Huang, YJ, Cort, JR, Goldsmith-Fischman, S, Xiao, R, Shih, L-Y, Ho, CK, Liu, J, Rost, B, Honig, B, Kennedy, MA, Acton, TB, Montelione, GT
JournalProtein Sci
Date Published2003 Dec
KeywordsAmino Acid Sequence, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Pyrococcus horikoshii, Ribosomal Proteins, Sequence Alignment

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 beta-sheet with a classic Greek-key topology and an oligonucleotide/oligosaccharide beta-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.

Alternate JournalProtein Sci.
PubMed ID14627742
PubMed Central IDPMC2366990
Grant ListP50 GM62413 / GM / NIGMS NIH HHS / United States