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Structure paper

TitleA Remote Palm Domain Residue of RB69 DNA Polymerase Is Critical for Enzyme Activity and Influences the Conformation of the Active Site.
Journal, issue, pagesPlos One, Vol. 8, Page e76700-e76700, Year 2013
Publish dateDec 5, 2012 (structure data deposition date)
AuthorsJacewicz, A. / Trzemecka, A. / Guja, K.E. / Plochocka, D. / Yakubovskaya, E. / Bebenek, A. / Garcia-Diaz, M.
External linksPlos One / PubMed:24116139
MethodsX-ray diffraction
Resolution2.3 - 2.6 Å
Structure data

PDB-4i9l:
Crystal structure of the D714A mutant of RB69 DNA polymerase
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-4i9q:
Crystal structure of the ternary complex of the D714A mutant of RB69 DNA polymerase
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-4khn:
Crystal structure of the ternary complex of the D714A mutant of RB69 DNA polymerase
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

Chemicals

ChemComp-GMP:
GUANOSINE

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-XG4:
2'-deoxy-5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]guanosine

ChemComp-CA:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • enterobacteria phage rb69 (virus)
  • synthetic construct (others)
KeywordsHYDROLASE / TRANSFERASE / PALM SUBDOMAIN / TRANSFERASE/DNA / TRANSFERASE-DNA complex

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