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Structure paper

TitletRNAHis guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 107, Page 20305-20310, Year 2010
Publish dateSep 11, 2010 (structure data deposition date)
AuthorsHyde, S.J. / Eckenroth, B.E. / Smith, B.A. / Eberley, W.A. / Heintz, N.H. / Jackman, J.E. / Doublie, S.
External linksProc. Natl. Acad. Sci. USA / PubMed:21059936
MethodsX-ray diffraction
Resolution2.28 - 3.01 Å
Structure data

PDB-3otb:
Crystal structure of human tRNAHis guanylyltransferase (Thg1) - dGTP complex
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-3otc:
Crystal structure of human tRNAHis guanylyltransferase (Thg1)- Native II
Method: X-RAY DIFFRACTION / Resolution: 3.01 Å

PDB-3otd:
Crystal structure of human tRNAHis guanylyltransferase (Thg1)- NaI derivative
Method: X-RAY DIFFRACTION / Resolution: 2.28 Å

PDB-3ote:
Crystal structure of human tRNAHis guanylyltransferase (Thg1)- Native I
Method: X-RAY DIFFRACTION / Resolution: 2.56 Å

Chemicals

ChemComp-DGT:
2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-3PO:
TRIPHOSPHATE

ChemComp-IOD:
IODIDE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / guanylyltransferase / polymerase-like palm domain / catalytic carboxylates

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