1NY4
Solution structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii. Northeast Structural Genomics Consortium target JR19.
Summary for 1NY4
Entry DOI | 10.2210/pdb1ny4/pdb |
NMR Information | BMRB: 5691 |
Descriptor | 30S ribosomal protein S28E (1 entity in total) |
Functional Keywords | jr19, autostructure, ribosomal protein, northeast structural genomics consortium, psi, protein structure initiative, nesg, rna binding protein |
Biological source | Pyrococcus horikoshii |
Total number of polymer chains | 1 |
Total formula weight | 9386.69 |
Authors | Aramini, J.M.,Cort, J.R.,Huang, Y.J.,Xiao, R.,Acton, T.B.,Ho, C.K.,Shih, L.-Y.,Kennedy, M.A.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2003-02-11, release date: 2003-09-02, Last modification date: 2024-05-22) |
Primary citation | Aramini, J.M.,Huang, Y.J.,Cort, J.R.,Goldsmith-Fischman, S.,Xiao, R.,Shih, L.-Y.,Ho, C.K.,Liu, J.,Rost, B.,Honig, B.,Kennedy, M.A.,Acton, T.B.,Montelione, G.T. Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii. Protein Sci., 12:2823-2830, 2003 Cited by PubMed 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 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. PubMed: 14627742DOI: 10.1110/ps.03359003 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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