1ZEL

Crystal structure of RV2827C protein from Mycobacterium tuberculosis

Summary for 1ZEL

• Entry DOI: 10.2210/pdb1zel/pdb
• Descriptor: hypothetical protein Rv2827c, SODIUM ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (6 entities in total)
• Functional Keywords: rv2827c, hypothetical protein, winged-helix, helix-turn-helix, auto-rickshaw, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, unknown function
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 66201.54

Authors

Janowski, R.,Panjikar, S.,Mueller-dieckmann, J.,Weiss, M.S.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2005-04-19, release date: 2006-05-02, Last modification date: 2024-02-14)

Primary citation

Janowski, R.,Panjikar, S.,Eddine, A.N.,Kaufmann, S.H.,Weiss, M.S.
Structural analysis reveals DNA binding properties of Rv2827c, a hypothetical protein from Mycobacterium tuberculosis.
J Struct Funct Genomics, 10:137-150, 2009

PubMed 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 A. 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.

PubMed: 19184528
DOI: 10.1007/s10969-009-9060-4

Experimental method

X-RAY DIFFRACTION (1.93 Å)