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1NY4

Solution structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii. Northeast Structural Genomics Consortium target JR19.

Summary for 1NY4
Entry DOI10.2210/pdb1ny4/pdb
NMR InformationBMRB: 5691
Descriptor30S ribosomal protein S28E (1 entity in total)
Functional Keywordsjr19, autostructure, ribosomal protein, northeast structural genomics consortium, psi, protein structure initiative, nesg, rna binding protein
Biological sourcePyrococcus horikoshii
Total number of polymer chains1
Total formula weight9386.69
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 citationAramini, 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: 14627742
DOI: 10.1110/ps.03359003
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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數據於2024-11-06公開中

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