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Structure of family X DNA polymerase from Deinococcus radioduransStructure of family X DNA polymerase from Deinococcus radiodurans
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDeinococcus radiodurans is an extraordinarily radioresistant bacterium which is able to repair hundreds of radiation-induced double-stranded DNA breaks. One of the players in this pathway is an X family DNA polymerase (PolXDr). Deletion of PolXDr has been shown to decrease the rate of repair of double-stranded DNA breaks and increase cell sensitivity to gamma-rays. A 3'5' exonuclease activity that stops cutting close to DNA loops has also been demonstrated. The present crystal structure of PolXDr solved at 2.46 A resolution reveals that PolXDr has a novel extended conformation in stark contrast to the closed "right hand" conformation commonly observed for DNA polymerases. This extended conformation is stabilized by the C-terminal PHP domain, whose putative nuclease active site is obstructed by its interaction with the polymerase domain. The overall conformation and the presence of non standard residues in the active site of the polymerase X domain makes PolXDr the founding member of a novel class of polymerases involved in DNA repair but whose detailed mode of action still remains enigmatic. The family X DNA polymerase from deinococcus radiodurans adopts a non-standard extended conformation.,Leulliot N, Cladiere L, Lecointe F, Durand D, Hubscher U, van Tilbeurgh H J Biol Chem. 2009 Feb 26. PMID:19251692[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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