Structural analysis reveals DNA binding properties of Rv2827c, a hypothetical protein from Mycobacterium tuberculosis

Robert Janowski, Santosh Panjikar, Ali Nasser Eddine, Stefan H.E. Kaufmann, Manfred S. Weiss

Research output: Contribution to journalArticleResearchpeer-review

10 Citations (Scopus)

Abstract

Tuberculosis (TB) is a major global health threat caused by Mycobacterium tuberculosis (Mtb). It is further fueled by the HIV pandemic and by increasing incidences of multidrug resistant Mtb-strains. Rv2827c, a hypothetical protein from Mtb, has been implicated in the survival of Mtb in the macrophages of the host. The three-dimensional structure of Rv2827c has been determined by the three-wavelength anomalous diffraction technique using bromide-derivatized crystals and refined to a resolution of 1.93 Å. The asymmetric unit of the orthorhombic crystals contains two independent protein molecules related by a non-crystallographic translation. The tertiary structure of Rv2827c comprises two domains: an N-terminal domain displaying a winged helix topology and a C-terminal domain, which appears to constitute a new and unique fold. Based on structural homology considerations and additional biochemical evidence, it could be established that Rv2827c is a DNA-binding protein. Once the understanding of the structure-function relationship of Rv2827c extends to the function of Rv2827c in vivo, new clues for the rational design of novel intervention strategies may be obtained.

Original languageEnglish
Pages (from-to)137-150
Number of pages14
JournalJournal of Structural and Functional Genomics
Volume10
Issue number2
DOIs
Publication statusPublished - Apr 2009
Externally publishedYes

Keywords

  • DNA binding
  • Hypothetical protein
  • Mycobacterium tuberculosis
  • Rv2827c
  • Winged helix domain
  • X-ray crystallography

Cite this