TY - JOUR
T1 - Structural analysis reveals DNA binding properties of Rv2827c, a hypothetical protein from Mycobacterium tuberculosis
AU - Janowski, Robert
AU - Panjikar, Santosh
AU - Eddine, Ali Nasser
AU - Kaufmann, Stefan H.E.
AU - Weiss, Manfred S.
PY - 2009/4
Y1 - 2009/4
N2 - 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.
AB - 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.
KW - DNA binding
KW - Hypothetical protein
KW - Mycobacterium tuberculosis
KW - Rv2827c
KW - Winged helix domain
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=62949101921&partnerID=8YFLogxK
U2 - 10.1007/s10969-009-9060-4
DO - 10.1007/s10969-009-9060-4
M3 - Article
C2 - 19184528
AN - SCOPUS:62949101921
VL - 10
SP - 137
EP - 150
JO - Journal of Structural and Functional Genomics
JF - Journal of Structural and Functional Genomics
SN - 1345-711X
IS - 2
ER -