3B54

Saccharomyces cerevisiae nucleoside diphosphate kinase

Summary for 3B54

• Entry DOI: 10.2210/pdb3b54/pdb
• Descriptor: Nucleoside diphosphate kinase, PHOSPHATE ION (3 entities in total)
• Functional Keywords: alpha/beta sandwich, atp-binding, kinase, magnesium, metal-binding, mitochondrion, nucleotide metabolism, nucleotide-binding, phosphorylation, transferase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm: P36010
• Total number of polymer chains: 2
• Total formula weight: 36607.55

Authors

Wang, H.B.,Bao, R.,Cheng, Y.X. (deposition date: 2007-10-25, release date: 2008-10-07, Last modification date: 2023-11-01)

Primary citation

Wang, H.,Bao, R.,Jiang, C.,Yang, Z.,Zhou, C.-Z.,Chen, Y.
Structure of Ynk1 from the yeast Saccharomyces cerevisiae
Acta Crystallogr.,Sect.F, 64:572-576, 2008

PubMed Abstract: Nucleoside diphosphate kinase (NDPK) catalyzes the transfer of the gamma-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 A resolution. Structural analysis strongly supports the oligomerization state of this protein being hexameric rather than tetrameric.

PubMed: 18607079
DOI: 10.1107/S1744309108015212

Experimental method

X-RAY DIFFRACTION (3.1 Å)