4.3 Article

Quaternary structure of nucleoside diphosphate kinases

Journal

JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
Volume 32, Issue 3, Pages 227-236

Publisher

SPRINGER/PLENUM PUBLISHERS
DOI: 10.1023/A:1005580828141

Keywords

NDP kinase; subunit interaction; quaternary structure; evolution; mixed oligomers; Dictyostelium

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Nucleoside (NDP) diphosphate kinases are oligomeric enzymes. Most are hexameric, but some bacterial enzymes are tetrameric. Hexamers and tetramers are constructed by assembling identical dimers. The hexameric structure is important for protein stability, as demonstrated by studies with natural mutants (the Killer-of-prune mutant of Drosophila NDP kinase and the S120G mutant of the human NDP kinase A in neuroblastomas) and with mutants obtained by site-directed mutagenesis. It is also essential for enzymic activity. The function of the tetrameric structure is unclear.

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