Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus

Mischa Machius, Lisa Henry, Maya Palnitkar, Johann Deisenhofer

Research output: Contribution to journalArticle

87 Citations (Scopus)

Abstract

Nucleotide excision repair (NER) is the most important DNA-repair mechanism in living organisms. In prokaryotes, three enzymes forming the UvrABC system initiate NER of a variety of structurally different DNA lesions, UvrB, the central component of this system, is responsible for the ultimate DNA damage recognition and participates in the incision of the damaged DNA strand. The crystal structure of Thermus thermophilus UvrB reveals a core that is structurally similar to core regions found in helicases, where they constitute molecular motors. Additional domains implicated in binding to DNA and various components of the NER system are attached to this central core. The architecture and distribution of DNA binding sites suggest a possible model for the DNA damage recognition process.

Original languageEnglish (US)
Pages (from-to)11717-11722
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number21
DOIs
StatePublished - Oct 12 1999

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Thermus thermophilus
DNA Repair
DNA
Enzymes
DNA Damage
Binding Sites

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus. / Machius, Mischa; Henry, Lisa; Palnitkar, Maya; Deisenhofer, Johann.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 21, 12.10.1999, p. 11717-11722.

Research output: Contribution to journalArticle

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