X‐ray structure of Mycobacterium tuberculosis nucleoside diphosphate kinase

Hydrogen/Deuterium Exchange Mass Spectrometry Reveals Mechanistic Details of Activation of Nucleoside Diphosphate Kinases by Oligomerization

“…(49) In addition to its kinase function, Mt-NDPK binds DNA (55) and also blocks phagosome maturation in murine macrophages leading to evasion of innate immunity. (56) The escape mechanism is unknown, but efficient intracellular survival of Mt requires a strong thermodynamic stability of proteins.…”

“…In addition, the stabilization of hexamers by subunit interactions has been studied. (49)(50)(51)(52)(53) Crystallographic structures of several-NDPK mutants provide detailed understanding of the WT stabilization mechanism, (53,54) but provide little understanding as to why oligomerization is necessary for function. So, we realized that by combining stability aspects with the study of their dynamic properties, we would improve this understanding.…”

Crystal structure of nucleoside diphosphate kinase required for coleoptile elongation in rice (Oryza sativa L.)

“…Although NDK sequences in various species are highly conserved, there are variations in their tertiary structures. Several crystal structures of NDKs from eukaryotes were previously determined and reported in the PDB, such as those of D. discoideum , Drosophila (Chiadmi et al, 1993), humans (Moréra et al, 1995;Webb et al, 1995), and Arabidopsis thaliana (Im et al, 2004), as well as those from the prokaryotes including M. xanthus (Williams et al, 1993) and Mycobacterium tuberculosis (Chen et al, 2002). The Wrst structure of an NDK from a moderate halophile and Gram-positive bacterium Bacillus halodenitriWcans was determined as a hexamer .…”

Structural Analysis of Arabidopsis thaliana Nucleoside Diphosphate Kinase-2 for Phytochrome-mediated Light Signaling

“…[6][7][8][9][10][11][12][13][14] The eukaryotic enzymes are homohexamers, whereas several of the prokaryotic enzymes are homotetramers. 15 Whether tetramer or hexamer, the NDPK active sites are structurally identical, and almost all the residues involved in the active site are fully invariant from bacteria to humans.…”