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PDBsum entry 3si8

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protein dna_rna ligands metals links
Transferase/DNA PDB id
3si8

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
422 a.a.
DNA/RNA
Ligands
DZ4
GOL ×8
3D1
DTT ×2
EDO ×5
Metals
_CO
_MG ×2
Waters ×126
PDB id:
3si8
Name: Transferase/DNA
Title: Human DNA polymerase eta - DNA ternary complex with the 5't of a cpd in the active site (tt2)
Structure: DNA polymerase eta. Chain: a. Fragment: unp residues 1-432. Synonym: rad30 homolog a, xeroderma pigmentosum variant type protein. Engineered: yes. DNA (5'-d( Tp A Ap Cp (Ttd)p Ap Tp Gp Ap Cp Gp C)-3'). Chain: t. Engineered: yes. Other_details: DNA template (chain t).
Source: Homo sapiens. Human. Organism_taxid: 9606. Strain: chemically synthesized. Gene: polh, rad30, rad30a, xpv. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: DNA oligonucleotide with thymine dimer (cyclobutane
Resolution:
2.15Å     R-factor:   0.241     R-free:   0.258
Authors: C.Biertumpfel,Y.Zhao,Y.Kondo,S.Ramon-Maiques,M.Gregory,J.Y.Lee, C.Masutani,A.R.Lehmann,F.Hanaoka,W.Yang
Key ref: C.Biertümpfel et al. (2010). Structure and mechanism of human DNA polymerase eta. Nature, 465, 1044-1048. PubMed id: 20577208
Date:
17-Jun-11     Release date:   03-Aug-11    
Supersedes: 3mr4
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9Y253  (POLH_HUMAN) -  DNA polymerase eta from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
713 a.a.
422 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

DNA/RNA chains
  A-C-TTD-A-T-G-A-C-G-C 10 bases
  T-G-C-G-T-C-A-T-A 9 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    
 
 
Nature 465:1044-1048 (2010)
PubMed id: 20577208  
 
 
Structure and mechanism of human DNA polymerase eta.
C.Biertümpfel, Y.Zhao, Y.Kondo, S.Ramón-Maiques, M.Gregory, J.Y.Lee, C.Masutani, A.R.Lehmann, F.Hanaoka, W.Yang.
 
  ABSTRACT  
 
The variant form of the human syndrome xeroderma pigmentosum (XPV) is caused by a deficiency in DNA polymerase eta (Poleta), a DNA polymerase that enables replication through ultraviolet-induced pyrimidine dimers. Here we report high-resolution crystal structures of human Poleta at four consecutive steps during DNA synthesis through cis-syn cyclobutane thymine dimers. Poleta acts like a 'molecular splint' to stabilize damaged DNA in a normal B-form conformation. An enlarged active site accommodates the thymine dimer with excellent stereochemistry for two-metal ion catalysis. Two residues conserved among Poleta orthologues form specific hydrogen bonds with the lesion and the incoming nucleotide to assist translesion synthesis. On the basis of the structures, eight Poleta missense mutations causing XPV can be rationalized as undermining the molecular splint or perturbing the active-site alignment. The structures also provide an insight into the role of Poleta in replicating through D loop and DNA fragile sites.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22562137 A.Ummat, O.Rechkoblit, R.Jain, J.Roy Choudhury, R.E.Johnson, T.D.Silverstein, A.Buku, S.Lone, L.Prakash, S.Prakash, and A.K.Aggarwal (2012).
Structural basis for cisplatin DNA damage tolerance by human polymerase η during cancer chemotherapy.
  Nat Struct Mol Biol, 19, 628-632.
PDB code: 4eey
22358330 J.E.Sale, A.R.Lehmann, and R.Woodgate (2012).
Y-family DNA polymerases and their role in tolerance of cellular DNA damage.
  Nat Rev Mol Cell Biol, 13, 141-152.  
22785315 T.Nakamura, Y.Zhao, Y.Yamagata, Y.J.Hua, and W.Yang (2012).
Watching DNA polymerase η make a phosphodiester bond.
  Nature, 487, 196-201.
PDB codes: 4ecq 4ecr 4ecs 4ect 4ecu 4ecv 4ecw 4ecx 4ecy 4ecz 4ed0 4ed1 4ed2 4ed3 4ed6 4ed7 4ed8
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. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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