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Small-angle X-ray scattering reveals architecture and A2B2 stoichiometry of the UvrA-UvrB DNA damage sensor

  • Harvard University

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

The UvrA-UvrB (AB) protein complex operates in the bacterial nucleotide excision repair pathway as the main sensor of DNA damage. Crystallographic analysis of the AB complex revealed a linear UvrB-UvrA-UvrA-UvrB arrangement of subunits with an internal two-fold axis that became incorporated into the crystal. Here, we have used small-angle X-ray scattering (SAXS) to show close correspondence between the crystal structure and the entity in solution. This result confirms the number and disposition of subunits in the crystallographic model and rules out other possible arrangements suggested by packing in the crystal. The current SAXS analysis failed to detect significant changes to the structure as a function of nucleotide. Proteins 2013.

Original languageEnglish
Pages (from-to)132-139
Number of pages8
JournalProteins: Structure, Function and Bioinformatics
Volume81
Issue number1
DOIs
Publication statusPublished - Jan 2013
Externally publishedYes

Keywords

  • DNA damage repair
  • Hybrid methods
  • Nucleotide excision repair
  • Small-angle X-ray scattering
  • UvrA
  • UvrB

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