User:Karl E. Zahn/Sandbox RB69 1/domain-structure

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DNA polymerases (pols) are a specialized class of transferase enzymes that catalyze template directed extension of a primed DNA strand from free deoxynucleoside triphosphates. The family B DNA pol encoded in the genome of the bacteriophage RB69 represents such an enzyme that shares significant homology with the human primase associated pol α, the human replicative pols δ and ε, and the human repair pol ζ. The relative ease with which one can induce RB69 pol to form diffraction quality crystals in complex with DNA, in addition to its homology shared with important human enzymes, has allowed RB69 pol to serve as an extremely useful structural tool and model enzyme.

Domain topology of the apo structure of RB69 DNA polymerase (PDBID 1WAJ). N-terminal domain appears in blue, exo domain in red, palm in cyan, fingers in magenta, thumb in green.

Drag the structure with the mouse to rotate

The first crystal structure of RB69 pol, solved in 1997, revealed the domain topology characteristic of polymerases: the palm, fingers, and thumb domains obtain a spatial arrangement reminiscent of a . RB69 pol also wields intrinsic 3'→5' exonuclease proofreading activity, which drastically improves the fidelity of this enzyme and occurs in most replicative pols. An N-terminal domain precedes the exonuclease domain in primary sequence, bringing the total to .[1]

Use the links below to explore the five domains of RB69 pol!

References

  1. ↑ Wang J, Sattar AK, Wang CC, Karam JD, Konigsberg WH, Steitz TA. Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69. Cell. 1997 Jun 27;89(7):1087-99. PMID:9215631

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Karl E. Zahn

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