Related ArticlesRibosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Biochemistry. 1993 Nov 30;32(47):12812-20
Authors: Golden BL, Hoffman DW, Ramakrishnan V, White SW
The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The 1H and 15N chemical shift assignments are largely complete, and a preliminary structural characterization is presented. The protein consists of five beta-strands that form a single antiparallel beta-sheet with Greek-key topology. The beta-strands are connected by several extended loops, and two of these contain residue types that are frequently seen in the RNA-binding sites of proteins. Additionally, two point mutations that affect antibiotic resistance, translational fidelity, and ribosome assembly are located in these two regions of the protein. Since these potential RNA-binding sites are distributed over a large surface of the protein, it appears that the molecule may interact with several regions of 16S rRNA.
[NMR paper] Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Related Articles Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Protein Sci. 2003 Dec;12(12):2823-30
Authors: Aramini JM, Huang YJ, Cort JR, Goldsmith-Fischman S, Xiao R, Shih LY, Ho CK, Liu J, Rost B, Honig B, Kennedy MA, Acton TB, Montelione GT
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...
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[NMR paper] NMR structure of the ribosomal protein L23 from Thermus thermophilus.
NMR structure of the ribosomal protein L23 from Thermus thermophilus.
Related Articles NMR structure of the ribosomal protein L23 from Thermus thermophilus.
J Biomol NMR. 2003 Jun;26(2):131-7
Authors: Ohman A, Rak A, Dontsova M, Garber MB, Härd T
The ribosomal protein L23 is a component of the large ribosomal subunit in which it is located close to the peptide exit tunnel. In this position L23 plays a central role both for protein secretion and folding. We have determined the solution structure of L23 from Thermus thermophilus. Uncomplexed L23...
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[NMR paper] NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly
NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.
Related Articles NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.
J Mol Biol. 2002 Oct 11;323(1):143-51
Authors: Raibaud S, Lebars I, Guillier M, Chiaruttini C, Bontems F, Rak A, Garber M, Allemand F, Springer M, Dardel F
L20 is a specific protein of the bacterial ribosome, which is involved in the early assembly steps of the 50S subunit and in the feedback control of the...
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[NMR paper] Refining the overall structure and subdomain orientation of ribosomal protein S4 delt
Refining the overall structure and subdomain orientation of ribosomal protein S4 delta41 with dipolar couplings measured by NMR in uniaxial liquid crystalline phases.
Related Articles Refining the overall structure and subdomain orientation of ribosomal protein S4 delta41 with dipolar couplings measured by NMR in uniaxial liquid crystalline phases.
J Mol Biol. 1999 Sep 17;292(2):375-87
Authors: Markus MA, Gerstner RB, Draper DE, Torchia DA
Prokaryotic protein S4 initiates assembly of the small ribosomal subunit by binding to 16 S rRNA....
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[NMR paper] NMR structure determination of the binding site for ribosomal protein S8 from Escheri
NMR structure determination of the binding site for ribosomal protein S8 from Escherichia coli 16 S rRNA.
Related Articles NMR structure determination of the binding site for ribosomal protein S8 from Escherichia coli 16 S rRNA.
J Mol Biol. 1998 Jul 24;280(4):639-54
Authors: Kalurachchi K, Nikonowicz EP
Many cellular processes involve the preferential interaction of an RNA molecule with a specific protein. A detailed analysis of the individual protein and RNA components of these interactions can provide unique insights into the structural...
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[NMR paper] Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spec
Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy.
Related Articles Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy.
Int J Pept Protein Res. 1996 Apr;47(4):282-8
Authors: Katahira R, Flotow H, Thomas G, Nosaka AY
An increase in the rate of protein synthesis is found to be accompanied by phosphorylation of the 40S ribosomal protein S6. Treatment of S6 by cyanogen bromide produced three fragments, and one of the fragments of S6, which is a C-terminal...
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[NMR paper] Ribosomal protein L9: a structure determination by the combined use of X-ray crystall
Ribosomal protein L9: a structure determination by the combined use of X-ray crystallography and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Ribosomal protein L9: a structure determination by the combined use of X-ray crystallography and NMR spectroscopy.
J Mol Biol. 1996 Dec 20;264(5):1058-71
Authors: Hoffman DW, Cameron CS, Davies C, White SW, Ramakrishnan V
The structure of protein L9 from the Bacillus stearothernophilus ribosome has been...
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[NMR paper] Characterization of the three-dimensional solution structure of human profilin: 1H, 1
Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern.
Related Articles Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern.
Biochemistry. 1993 Dec 21;32(50):13818-29
Authors: Metzler WJ, Constantine KL, Friedrichs MS, Bell AJ, Ernst EG, Lavoie TB, Mueller L
Human profilin is a 15-kDa protein that plays a major role in the signaling pathway leading to cytoskeletal...