Premium
Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii
Author(s) -
Aramini James M.,
Huang Yuanpeng J.,
Cort John R.,
GoldsmithFischman Sharon,
Xiao Rong,
Shih LiangYu,
Ho Chi K.,
Liu Jinfeng,
Rost Burkhard,
Honig Barry,
Kennedy Michael A.,
Acton Thomas B.,
Montelione Gaetano T.
Publication year - 2003
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.03359003
Subject(s) - pyrococcus horikoshii , structural genomics , ribosomal protein , 30s , crystallography , nuclear magnetic resonance spectroscopy , 5.8s ribosomal rna , chemistry , ribosomal rna , protein structure , stereochemistry , biochemistry , biology , rna , gene , ribosome , crystal structure
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.