Open AccessStructure of Ynk1 from the yeast Saccharomyces cerevisiae
Author(s) -
Wang Huabing,
Bao Rui,
Jiang Chunhui,
Yang Zhu,
Zhou CongZhao,
Chen Yuxing
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108015212
Subject(s) - nucleoside diphosphate kinase , saccharomyces cerevisiae , nucleoside , yeast , nucleotide , biochemistry , chemistry , stereochemistry , biology , enzyme , gene
Nucleoside diphosphate kinase (NDPK) catalyzes the transfer of the γ‐phosphate from nucleoside triphosphates to nucleoside diphosphates. In addition to biochemical studies, a number of crystal structures of NDPK from various organisms, including both native proteins and complexes with nucleotides or nucleotide analogues, have been determined. Here, the crystal structure of Ynk1, an NDPK from the yeast Saccharomyces cerevisiae , has been solved at 3.1 Å resolution. Structural analysis strongly supports the oligomerization state of this protein being hexameric rather than tetrameric.