NMR assignment and secondary structure identification of the ribosomal protein
L11 from Thermotoga maritima

L11 is in the free, non-RNA bound state.
Thermotoga maritima Ribosomal protein L11

NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.

Markus MA, Triantafillidou D, Choli-Papadopoulou T, Torchia DA.
1H, 15N, and 13C assignments and secondary structure identification for
full-length ribosomal protein L11 from Thermus thermophilus.
J Biomol NMR. 2001 Jul;20(3):293-4.

1H, 15N, and 13C assignments and secondary structure identification for full-length ribosomal protein L11 from Thermus thermophilus.

We report the crystal structure of a 58 nucleotide fragment of 23S ribosomal RNA
bound to ribosomal protein L11. This highly conserved ribonucleoprotein domain
is the target for the thiostrepton family of antibiotics that disrupt
elongation factor function. The highly compact RNA has both familiar and novel
structural motifs. While the C-terminal domain of L11 binds RNA tightly, the
N-terminal domain makes only limited contacts with RNA and is proposed to
function as a switch that reversibly associates with an adjacent region of RNA.
The sites of mutations conferring resistance to thiostrepton and micrococcin
line a narrow cleft between the RNA and the N-terminal domain. These
antibiotics are proposed to bind in this cleft, locking the putative switch and
interfering with the function of elongation factors.

Wimberly BT, Guymon R, McCutcheon JP, White SW, Ramakrishnan V.
A detailed view of a ribosomal active site: the structure of the L11-RNA
complex.
Cell. 1999 May 14;97(4):491-502.

A detailed view of a ribosomal active site: the structure of the L11-RNA complex.

The three-dimensional solution structure has been determined by NMR spectroscopy
of the 75 residue C-terminal domain of ribosomal protein L11 (L11-C76) in its
RNA-bound state. L11-C76 recognizes and binds tightly to a highly conserved 58
nucleotide domain of 23 S ribosomal RNA, whose secondary structure consists of
three helical stems and a central junction loop. The NMR data reveal that the
conserved structural core of the protein, which consists of a bundle of three
alpha-helices and a two-stranded parallel beta-sheet four residues in length,
is nearly the same as the solution structure determined for the non-liganded
form of the protein. There are however, substantial chemical shift
perturbations which accompany RNA binding, the largest of which map onto an
extended loop which bridges the C-terminal end of alpha-helix 1 and the first
strand of parallel beta-sheet. Substantial shift perturbations are also
observed in the N-terminal end of alpha-helix 1, the intervening loop that
bridges helices 2 and 3, and alpha-helix 3. The four contact regions identified
by the shift perturbation data also displayed protein-RNA NOEs, as identified
by isotope-filtered three-dimensional NOE spectroscopy. The shift perturbation
and NOE data not only implicate helix 3 as playing an important role in RNA
binding, but also indicate that regions flanking helix 3 are involved as well.
Loop 1 is of particular interest as it was found to be flexible and disordered
for L11-C76 free in solution, but not in the RNA-bound form of the protein,
where it appears rigid and adopts a specific conformation as a result of its
direct contact to RNA.

Hinck AP, Markus MA, Huang S, Grzesiek S, Kustonovich I, Draper DE, Torchia DA.
The RNA binding domain of ribosomal protein L11: three-dimensional structure
of the RNA-bound form of the protein and its interaction with 23 S rRNA.
J Mol Biol. 1997 Nov 21;274(1):101-13.

The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA.

Fitting Of Components With Known Structure Into An 11.5 A Cryo-Em Map Of The E.Coli 70s Ribosome

Crystal Structure Of The Ribosome At 5.5 A Resolution. This File, 1giy, Contains The 50s Ribosome Subunit. The 30s Ribosome Sub

Fitting Of L11 Protein And Elongation Factor G (Ef-G) In The Cryo-Em Map Of E. Coli 70s Ribosome Bound With Ef-G, Gdp And Fusid

Fitting Of L11 Protein And Elongation Factor G (Domain G' And V) In The Cryo-Em Map Of E. Coli 70s Ribosome Bound With Ef-G And

Fitting Of L11 Protein In The Low Resolution Cryo-Em Map Of E.Coli 70s Ribosome

Fitting The Ternary Complex Of Ef-TuTRNAGTP AND RIBOSOMAL PROTEINS Into A 13 A Cryo-Em Map Of The Coli 70s Ribosome

Structure Of The E. Coli Ribosomal Termination Complex With Release Factor 2

Crystal Structure Of The Ribosomal Protein L11-Rna Complex

Decoding Center & Peptidyl Transferase Center From The X-Ray Structure Of The Thermus Thermophilus 70s Ribosome, Aligned To The

Model For Thiostrepton Antibiotic Binding To L11 Substrate From 50s Ribosomal Rna

Coordinates Of S12, L11 Proteins And P-Trna, From The 70s X- Ray Structure Aligned To The 70s Cryo-Em Map Of E.Coli Ribosome

Coordinates Of S12, L11 Proteins And E-Site Trna From 70s Crystal Structure Separately Fitted Into The Cryo-Em Map Of E.Coli 70

Coordinates Of L11 With 58nts Of 23s Rrna Fitted Into The Cryo-Em Map Of The 70s Ribosome

Coordinates Of L11 With 58nts Of 23s Rrna Fitted Into The Cryo-em Map Of Ef-tu Ternary Complex (gdp.kirromycin) Bound 70s Ribos

Crystal Structure Of 70s Ribosome With Thrs Operator And Trnas. Large Subunit. The Coordinates For The Small Subunit Are In The

50s Ribosomal Subunit From A Crystal Structure Of Release Factor Rf1, Trnas And Mrna Bound To The Ribosome. This File Contains

50s Ribosomal Subunit From A Crystal Structure Of Release Factor Rf2, Trnas And Mrna Bound To The Ribosome. This File Contains

50s Ribosomal Subunit From A Crystal Structure Of The Ribosome In Complex With Trnas And Mrna With A Stop Codon In The A-Site.

Model For Thiostrepton Binding To The Ribosomal L11-Rna

Ribosomal Protein L11 From Thermotoga Maritima

Seven Ribosomal Proteins Fitted To A Cryo-Electron Microscopic Map Of The Large 50s Subunit At 7.5 Angstroms Resolution

ribosomal protein L11 [Thermotoga maritima MSB8]

LSU ribosomal protein L11P [Thermotoga petrophila RKU-1]

ribosomal protein L11 [Thermotoga sp. RQ2]

ribosomal protein L11 [Thermotoga naphthophila RKU-10]

LSU ribosomal protein L11p (L12e) [Thermotoga maritima MSB8]

50S ribosomal protein L11 [Thermotoga maritima MSB8]

MULTISPECIES: 50S ribosomal protein L11 [Thermotoga]

50S ribosomal protein L11 [Thermotoga petrophila RKU-1]

RecName: Full=50S ribosomal protein L11 [Thermotoga petrophila RKU-1]

RecName: Full=50S ribosomal protein L11 [Thermotoga sp. RQ2]

RecName: Full=50S ribosomal protein L11 [Thermotoga maritima MSB8]

Ch. Bartels, T.-H. Xia, M. Billeter, P. Guntert and K. Wuthrich (1995)
The program XEASY for computer-supported NMR spectral analysis of biological
macromolecules.
J. Biomolecular NMR 5, 1-10.