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Structure paper

TitleStructural and biochemical studies of TREX1 inhibition by metals. Identification of a new active histidine conserved in DEDDh exonucleases.
Journal, issue, pagesProtein Sci., Vol. 17, Page 2059-2069, Year 2008
Publish dateOct 29, 2007 (structure data deposition date)
AuthorsBrucet, M. / Querol-Audi, J. / Bertlik, K. / Lloberas, J. / Fita, I. / Celada, A.
External linksProtein Sci. / PubMed:18780819
MethodsX-ray diffraction
Resolution2.1 - 2.3 Å
Structure data

PDB-3b6o:
Structure of TREX1 in complex with a nucleotide and an inhibitor ion (lithium)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3b6p:
Structure of TREX1 in complex with a nucleotide and inhibitor ions (sodium and zinc)
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-LI:
Unknown entry

ChemComp-TMP:
THYMIDINE-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-NA:
Unknown entry

Source
  • mus musculus (house mouse)
KeywordsHYDROLASE / TREX1 / DEDD / exonuclease / DnaQ / lithium / catalysis / inhibition / deoxy-thimidine monophosphate (dTMP) / DNA damage / DNA repair / Magnesium / Nucleus / Phosphorylation / sodium / zinc

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