2VF7

Crystal structure of UvrA2 from Deinococcus radiodurans

Summary for 2VF7

• Entry DOI: 10.2210/pdb2vf7/pdb
• Related: 2VF8
• Descriptor: EXCINUCLEASE ABC, SUBUNIT A., ADENOSINE-5'-DIPHOSPHATE, ZINC ION, ... (5 entities in total)
• Functional Keywords: dna-binding protein, nucleotide-binding, zinc-binding domain, sos response, metal-binding, excision nuclease, zinc-finger, atp-binding, dna-binding, dna excision, zinc, cytoplasm, dna damage, dna repair, abc protein dna-binding protein, dna binding protein
• Biological source: DEINOCOCCUS RADIODURANS
• Total number of polymer chains: 3
• Total formula weight: 277973.63

Authors

Timmins, J.,Gordon, E.,Caria, S.,Leonard, G.,Kuo, M.S.,Monchois, V.,McSweeney, S. (deposition date: 2007-10-31, release date: 2008-12-16, Last modification date: 2024-05-08)

Primary citation

Timmins, J.,Gordon, E.,Caria, S.,Leonard, G.,Acajjaoui, S.,Kuo, M.S.,Monchois, V.,McSweeney, S.
Structural and mutational analyses of Deinococcus radiodurans UvrA2 provide insight into DNA binding and damage recognition by UvrAs.
Structure, 17:547-558, 2009

PubMed Abstract: UvrA proteins are key actors in DNA damage repair and play an essential role in prokaryotic nucleotide excision repair (NER), a pathway that is unique in its ability to remove a broad spectrum of DNA lesions. Understanding the DNA binding and damage recognition activities of the UvrA family is a critical component for establishing the molecular basis of this process. Here we report the structure of the class II UvrA2 from Deinococcus radiodurans in two crystal forms. These structures, coupled with mutational analyses and comparison with the crystal structure of class I UvrA from Bacillus stearothermophilus, suggest a previously unsuspected role for the identified insertion domains of UvrAs in both DNA binding and damage recognition. Taken together, the available information suggests a model for how UvrA interacts with DNA and thus sheds new light on the molecular mechanisms underlying the role of UvrA in the early steps of NER.

PubMed: 19368888
DOI: 10.1016/j.str.2009.02.008

Experimental method

X-RAY DIFFRACTION (2.3 Å)