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PDBsum entry 2jr4

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RNA PDB id
2jr4

 

 

 

 

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Contents
DNA/RNA
PDB id:
2jr4
Name: RNA
Title: Nmr solution structure of the anticodon of e.Coli tRNA-val3 with no modifications
Structure: 5'-r( Cp Cp Up Cp Cp Cp Up Up Ap Cp Ap Ap Gp Gp Ap Gp G)- 3'. Chain: a. Engineered: yes
Source: Synthetic: yes
NMR struc: 11 models
Authors: F.A.P.Vendeix,A.Dziergowska,E.M.Gustilo,W.D.Graham,B.Sproat, A.Malkiewicz,P.F.Agris
Key ref: F.A.Vendeix et al. (2008). Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding. Biochemistry, 47, 6117-6129. PubMed id: 18473483
Date:
20-Jun-07     Release date:   24-Jul-07    
 Headers
 References

DNA/RNA chain
  C-C-U-C-C-C-U-U-A-C-A-A-G-G-A-G-G 17 bases

 

 
Biochemistry 47:6117-6129 (2008)
PubMed id: 18473483  
 
 
Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding.
F.A.Vendeix, A.Dziergowska, E.M.Gustilo, W.D.Graham, B.Sproat, A.Malkiewicz, P.F.Agris.
 
  ABSTRACT  
 
The accuracy and efficiency with which tRNA decodes genomic information into proteins require posttranscriptional modifications in or adjacent to the anticodon. The modification uridine-5-oxyacetic acid (cmo (5)U 34) is found at wobble position 34 in a single isoaccepting tRNA species for six amino acids, alanine, leucine, proline, serine, threonine, and valine, each having 4-fold degenerate codons. cmo (5)U 34 makes possible the decoding of 24 codons by just six tRNAs. The contributions of this important modification to the structures and codon binding affinities of the unmodified and fully modified anticodon stem and loop domains of tRNA (Val3) UAC (ASL (Val3) UAC) were elucidated. The stems of the unmodified ASL (Val3) UAC and that with cmo (5)U 34 and N (6)-methyladenosine, m (6)A 37, adopted an A-form RNA conformation (rmsd approximately 0.6 A) as determined with NMR spectroscopy and torsion-angle molecular dynamics. However, the UV hyperchromicity, circular dichroism ellipticity, and structural analyses indicated that the anticodon modifications enhanced order in the loop. ASL (Val3) UAC-cmo (5)U 34;m (6)A 37 exhibited high affinities for its cognate and wobble codons GUA and GUG, and for GUU in the A-site of the programmed 30S ribosomal subunit, whereas the unmodified ASL (Val3) UAC bound less strongly to GUA and not at all to GUG and GUU. Together with recent crystal structures of ASL (Val3) UAC-cmo (5)U 34;m (6)A 37 bound to all four of the valine codons in the A-site of the ribosome's 30S subunit, these results clearly demonstrate that the xo (5)U 34-type modifications order the anticodon loop prior to A-site codon binding for an expanded codon reading, possibly reducing an entropic energy barrier to codon binding.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21193521 Z.Xu, and D.H.Mathews (2011).
Multilign: an algorithm to predict secondary structures conserved in multiple RNA sequences.
  Bioinformatics, 27, 626-632.  
20509917 H.Seligmann (2010).
Do anticodons of misacylated tRNAs preferentially mismatch codons coding for the misloaded amino acid?
  BMC Mol Biol, 11, 41.  
20403966 W.Ran, and P.G.Higgs (2010).
The influence of anticodon-codon interactions and modified bases on codon usage bias in bacteria.
  Mol Biol Evol, 27, 2129-2140.  
19383770 A.Y.Golovina, P.V.Sergiev, A.V.Golovin, M.V.Serebryakova, I.Demina, V.M.Govorun, and O.A.Dontsova (2009).
The yfiC gene of E. coli encodes an adenine-N6 methyltransferase that specifically modifies A37 of tRNA1Val(cmo5UAC).
  RNA, 15, 1134-1141.  
19861423 F.A.Vendeix, A.M.Munoz, and P.F.Agris (2009).
Free energy calculation of modified base-pair formation in explicit solvent: A predictive model.
  RNA, 15, 2278-2287.  
18927116 H.Lusic, E.M.Gustilo, F.A.Vendeix, R.Kaiser, M.O.Delaney, W.D.Graham, V.A.Moye, W.A.Cantara, P.F.Agris, and A.Deiters (2008).
Synthesis and investigation of the 5-formylcytidine modified, anticodon stem and loop of the human mitochondrial tRNAMet.
  Nucleic Acids Res, 36, 6548-6557.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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