spacer
spacer

PDBsum entry 4x4r

Go to PDB code: 
protein dna_rna ligands metals Protein-protein interface(s) links
RNA binding protein PDB id
4x4r

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
443 a.a.
DNA/RNA
Ligands
_DC-_DG
APC ×2
MES
GOL ×3
TAR
PEG
Metals
_MG ×2
PDB id:
4x4r
Name: RNA binding protein
Title: Crystal structure of the a.Fulgidus cca-adding enzyme in complex with a g70a arginyl-tRNA minihelix ending in ccacc and ampcpp
Structure: Cca-adding enzyme. Chain: a, c. Fragment: a. Fulgidus cca-adding enzyme. Synonym: cca tRNA nucleotidyltransferase,tRNA cca-pyrophosphorylase, tRNA adenylyl-/cytidylyl- transferase,tRNA nucleotidyltransferase, tRNA-nt. Engineered: yes. G70a tRNA minihelix ending in ccacc. Chain: b, d.
Source: Archaeoglobus fulgidus. Organism_taxid: 224325. Strain: atcc 49558 / vc-16 / dsm 4304 / jcm 9628 / nbrc 100126. Gene: cca, af_2156. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Homo sapiens. Organism_taxid: 9606.
Resolution:
3.20Å     R-factor:   0.212     R-free:   0.266
Authors: C.-D.Kuhn,L.Joshua-Tor
Key ref: C.D.Kuhn et al. (2015). On-enzyme refolding permits small RNA and tRNA surveillance by the CCA-adding enzyme. Cell, 160, 644-658. PubMed id: 25640237 DOI: 10.1016/j.cell.2015.01.005
Date:
03-Dec-14     Release date:   11-Feb-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O28126  (CCA_ARCFU) -  CCA-adding enzyme from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Seq:
Struc:
437 a.a.
443 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

DNA/RNA chains
  G-G-C-C-G-C-G-G-C-A-G-G-U-U-C-G-A-G-U-C-C-U-G-C-C-G-C-G-C-G-C-C-A-C-C 35 bases
  G-G-C-C-G-C-G-G-C-A-G-G-U-U-C-G-A-U-C-C-U-G-C-C-G-C-C-A-C-C 30 bases

 Enzyme reactions 
   Enzyme class: E.C.2.7.7.72  - Cca tRNA nucleotidyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate
tRNA precursor
+
2 × CTP
Bound ligand (Het Group name = APC)
matches with 55.00% similarity
+ ATP
= tRNA with a 3' CCA end
+ 3 × diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.cell.2015.01.005 Cell 160:644-658 (2015)
PubMed id: 25640237  
 
 
On-enzyme refolding permits small RNA and tRNA surveillance by the CCA-adding enzyme.
C.D.Kuhn, J.E.Wilusz, Y.Zheng, P.A.Beal, L.Joshua-Tor.
 
  ABSTRACT  
 
Transcription in eukaryotes produces a number of long noncoding RNAs (lncRNAs). Two of these, MALAT1 and Menβ, generate a tRNA-like small RNA in addition to the mature lncRNA. The stability of these tRNA-like small RNAs and bona fide tRNAs is monitored by the CCA-adding enzyme. Whereas CCA is added to stable tRNAs and tRNA-like transcripts, a second CCA repeat is added to certain unstable transcripts to initiate their degradation. Here, we characterize how these two scenarios are distinguished. Following the first CCA addition cycle, nucleotide binding to the active site triggers a clockwise screw motion, producing torque on the RNA. This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle. Intriguingly, with the CCA-adding enzyme acting as a molecular vise, the RNAs proofread themselves through differential responses to its interrogation between stable and unstable substrates.
 

 

spacer

spacer