Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 276, Issue 40, Pages 37443-37450Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M104285200
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Funding
- NIDDK NIH HHS [R01 DK047844, DK47844, R01 DK056898, DK56898] Funding Source: Medline
- NIGMS NIH HHS [R01 GM051262-09, R01 GM051262, GM51262, R29 GM051262] Funding Source: Medline
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The structure of mitochondrial pyruvate dehydrogenase kinase isozyme 2 is of interest because it represents a family of serine-specific protein kinases that lack sequence similarity with all other eukaryotic protein kinases. Similarity exists instead with key motifs of prokaryotic histidine protein kinases and a family of eukaryotic ATPases. The 2.5-Angstrom crystal structure reported here reveals that pyruvate dehydrogenase kinase isozyme 2 has two domains of about the same size. The N-terminal half is dominated by a bundle of four amphipathic alpha -helices, whereas the C-terminal half is folded into an alpha/beta sandwich that contains the nucleotide-binding site. Analysis of the structure reveals this C-terminal domain to be very similar to the nucleotide-binding domain of bacterial histidine kinases, but the catalytic mechanism appears similar to that of the eukaryotic serine kinases and ATPases.
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