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PDBsum entry 3tux

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protein ligands metals links
Transferase PDB id
3tux

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
336 a.a.
Ligands
ATP
SO4
GOL
EDO ×2
Metals
_MN
Waters ×311
PDB id:
3tux
Name: Transferase
Title: Crystal structure of rtca.Atp.Mn ternary complex
Structure: RNA 3'-terminal phosphate cyclase. Chain: a. Synonym: RNA cyclase, RNA-3'-phosphate cyclase. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b4475, jw5688, rtca, yhgj, yhgk. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.85Å     R-factor:   0.189     R-free:   0.252
Authors: A.K.Chakravarty,P.Smith,S.Shuman
Key ref: A.K.Chakravarty et al. (2011). Structures of RNA 3'-phosphate cyclase bound to ATP reveal the mechanism of nucleotidyl transfer and metal-assisted catalysis. Proc Natl Acad Sci U S A, 108, 21034-21039. PubMed id: 22167800
Date:
19-Sep-11     Release date:   28-Dec-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P46849  (RTCA_ECOLI) -  RNA 3'-terminal phosphate cyclase from Escherichia coli (strain K12)
Seq:
Struc:
338 a.a.
336 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.6.5.1.4  - Rna 3'-terminal-phosphate cyclase (ATP).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
3'-end 3'-phospho-ribonucleotide-RNA
+
ATP
Bound ligand (Het Group name = ATP)
corresponds exactly
= 3'-end 2',3'-cyclophospho-ribonucleotide-RNA
+ AMP
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Proc Natl Acad Sci U S A 108:21034-21039 (2011)
PubMed id: 22167800  
 
 
Structures of RNA 3'-phosphate cyclase bound to ATP reveal the mechanism of nucleotidyl transfer and metal-assisted catalysis.
A.K.Chakravarty, P.Smith, S.Shuman.
 
  ABSTRACT  
 
No abstract given.

 

 

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