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

James M. Aramini, Yuanpeng J. Huang, John R. Cort, Sharon Goldsmith-Fischman, Rong Xiao, Liang Yu Shih, Chi K. Ho, Jinfeng Liu, Burkhard Rost, Barry Honig, Michael A. Kennedy, Thomas B. Acton, Gaetano T. Montelione

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)2823-2830
Number of pages8
JournalProtein Science
Volume12
Issue number12
DOIs
StatePublished - Dec 2003

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Keywords

  • Greek-key motif
  • NMR structure
  • Northeast Structural Genomics Consortium
  • Ribosomal protein

Fingerprint Dive into the research topics of 'Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii'. Together they form a unique fingerprint.

Cite this