2W9M

Structure of family X DNA polymerase from Deinococcus radiodurans

Summary for 2W9M

• Entry DOI: 10.2210/pdb2w9m/pdb
• Descriptor: POLYMERASE X, ZINC ION, MERCURY (II) ION, ... (4 entities in total)
• Functional Keywords: saxs, dna repair, dna polymerase, dna replication
• Biological source: DEINOCOCCUS RADIODURANS
• Total number of polymer chains: 2
• Total formula weight: 125260.94

Authors

Leulliot, N.,Cladiere, L.,Lecointe, F.,Durand, D.,Hubscher, U.,van Tilbeurgh, H. (deposition date: 2009-01-27, release date: 2009-02-10, Last modification date: 2024-05-08)

Primary citation

Leulliot, N.,Cladiere, L.,Lecointe, F.,Durand, D.,Hubscher, U.,Van Tilbeurgh, H.
The Family X DNA Polymerase from Deinococcus Radioduran Adopts a Non-Standard Extended Conformation.
J.Biol.Chem., 284:11992-, 2009

PubMed Abstract: Deinococcus radiodurans is an extraordinarily radioresistant bacterium that 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 (PolX(Dr)). Deletion of PolX(Dr) 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 PolX(Dr) solved at 2.46-A resolution reveals that PolX(Dr) 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 PolX(Dr) the founding member of a novel class of polymerases involved in DNA repair but whose detailed mode of action still remains enigmatic.

PubMed: 19251692
DOI: 10.1074/JBC.M809342200

Experimental method

X-RAY DIFFRACTION (2.46 Å)