Related ArticlesRibosomal 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 determined at 2.5 A resolution by refinement against single crystal X-ray diffraction data with additional constraints provided by NMR data. This highly elongated protein consists of two domains separated by a nine-turn connecting helix. Conserved aromatic and positively charged amino acid residues on the surface of each domain are likely to be directly involved in binding 23 S ribosomal RNA. The shape of the protein, with its two widely spaced RNA-binding sites, suggests that it may serve as a "molecular strut", most likely playing a role in ribosome assembly and/or maintaining the catalytically active conformation of the ribosomal RNA. The combined use of X-ray and NMR data in the refinement procedure was essential in defining the N-terminal domain of the protein, which was relatively poorly determined by the X-ray data alone. In addition to resolving the ambiguities in defining the hydrophobic core and side-chain conformations with the N-terminal domain, this combined NMR-X-ray analysis provides the first detailed and accurate view of the N-terminal RNA-binding site. NMR data also showed that the N-terminal domain is stable in solution, indicated by amide protons that are protected from solvent exchange. The lack of definition of the N-terminal domain in the X-ray structure is therefore likely due to packing disorder within the crystal rather than structural instability. This combined NMR-X-ray analysis provides a useful model as to how X-ray and NMR data can be practically and logically combined in the determination of the structure of a single protein molecule.
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Related Articles Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Structure. 2010 Dec 8;18(12):1678-1687
Authors: Masica DL, Ash JT, Ndao M, Drobny GP, Gray JJ
Protein-biomineral interactions are paramount to materials production in biology, including the mineral phase of hard tissue. Unfortunately, the...
nmrlearner
Journal club
0
12-08-2010 06:21 PM
[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...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[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...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[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...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[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....
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[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...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[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...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] Ribosomal protein S17: characterization of the three-dimensional structure by 1H and
Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Related Articles Ribosomal 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...
Ribosomal protein L9: a structure determination by the combined use of X-ray crystall
Linear Mode
