Crystal structure and biophysical characterization of the nucleoside diphosphate kinase from Leishmania braziliensis.

ABSTRACT:

Background

Nucleoside diphosphate kinase (NDK) is a housekeeping enzyme that plays key roles in nucleotide recycling and homeostasis in trypanosomatids. It is also secreted by the intracellular parasite Leishmania to modulate the host response. These functions make NDK an attractive target for drug design and for studies aiming at a better understanding of the mechanisms mediating host-pathogen interactions.

Results

We report the crystal structure and biophysical characterization of the NDK from Leishmania braziliensis (LbNDK). The subunit consists of six α-helices along with a core of four β-strands arranged in a β2β3β1β4 antiparallel topology order. In contrast to the NDK from L. major, the LbNDK C-terminal extension is partially unfolded. SAXS data showed that LbNDK forms

SUBMITTER: Vieira PS 

PROVIDER: S-EPMC4322457 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature