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PDBsum entry 5ytc

Go to PDB code: 
protein dna_rna ligands metals links
Transferase/DNA PDB id
5ytc

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
539 a.a.
DNA/RNA
Ligands
DTP
Metals
_MG ×2
Waters ×262
PDB id:
5ytc
Name: Transferase/DNA
Title: Large fragment of DNA polymerase i from thermus aquaticus in a closed ternary complex with the unnatural base m-fc pair with datp in the active site
Structure: DNA polymerase i, thermostable. Chain: a. Fragment: large fragment. Synonym: taq polymerase 1. Engineered: yes. DNA (5'-d( Gp Ap Cp Cp Ap Cp Gp Gp Cp Gp Cp (Doc)p (Doc))- 3'). Chain: b. Engineered: yes.
Source: Thermus aquaticus. Organism_taxid: 271. Gene: pola, pol1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic construct. Organism_taxid: 32630. Organism_taxid: 32630
Resolution:
2.28Å     R-factor:   0.197     R-free:   0.258
Authors: H.Zeng,M.Mondal,R.Y.Song,J.Zhang,B.Xia,C.Q.Yi
Key ref: H.Zeng et al. (2019). Unnatural Cytosine Bases Recognized as Thymines by DNA Polymerases by the Formation of the Watson-Crick Geometry. Angew Chem Int Ed Engl, 58, 130-133. PubMed id: 30407705 DOI: 10.1002/anie.201807845
Date:
17-Nov-17     Release date:   21-Nov-18    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P19821  (DPO1_THEAQ) -  DNA polymerase I, thermostable from Thermus aquaticus
Seq:
Struc:
 
Seq:
Struc:
832 a.a.
539 a.a.
Key:    PfamA domain  Secondary structure

DNA/RNA chains
  G-A-C-C-A-C-G-G-C-G-C-DOC 12 bases
  A-A-A-92F-G-G-C-G-C-C-G-T-G-G-T-C 16 bases

 Enzyme reactions 
   Enzyme class: E.C.2.7.7.7  - DNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
DNA(n)
+ 2'-deoxyribonucleoside 5'-triphosphate
= DNA(n+1)
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1002/anie.201807845 Angew Chem Int Ed Engl 58:130-133 (2019)
PubMed id: 30407705  
 
 
Unnatural Cytosine Bases Recognized as Thymines by DNA Polymerases by the Formation of the Watson-Crick Geometry.
H.Zeng, M.Mondal, R.Song, J.Zhang, B.Xia, M.Liu, C.Zhu, B.He, Y.Q.Gao, C.Yi.
 
  ABSTRACT  
 
The emergence of unnatural DNA bases provides opportunities to demystify the mechanisms by which DNA polymerases faithfully decode chemical information on the template. It was previously shown that two unnatural cytosine bases (termed "M-fC" and "I-fC"), which are chemical labeling adducts of the epigenetic base 5-formylcytosine, can induce C-to-T transition during DNA amplification. However, how DNA polymerases recognize such unnatural cytosine bases remains enigmatic. Herein, crystal structures of unnatural cytosine bases pairing to dA/dG in the KlenTaq polymerase-host-guest complex system and pairing to dATP in the KlenTaq polymerase active site were determined. Both M-fC and I-fC base pair with dA/dATP, but not with dG, in a Watson-Crick geometry. This study reveals that the formation of the Watson-Crick geometry, which may be enabled by the A-rule, is important for the recognition of unnatural cytosines.
 

 

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