1JM6

Pyruvate dehydrogenase kinase, isozyme 2, containing ADP

Summary for 1JM6

• Entry DOI: 10.2210/pdb1jm6/pdb
• Descriptor: Pyruvate dehydrogenase kinase, isozyme 2, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: kinase, mitochondion, serine kinase, transferase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Mitochondrion matrix: Q64536
• Total number of polymer chains: 2
• Total formula weight: 93214.06

Authors

Steussy, C.N.,Popov, K.M.,Bowker-Kinley, M.M.,Sloan, R.B.,Harris, R.A.,Hamilton, J.A. (deposition date: 2001-07-17, release date: 2001-10-24, Last modification date: 2024-02-07)

Primary citation

Steussy, C.N.,Popov, K.M.,Bowker-Kinley, M.M.,Sloan Jr., R.B.,Harris, R.A.,Hamilton, J.A.
Structure of pyruvate dehydrogenase kinase. Novel folding pattern for a serine protein kinase.
J.Biol.Chem., 276:37443-37450, 2001

PubMed Abstract: 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-A 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.

PubMed: 11483605
DOI: 10.1074/jbc.M104285200

Experimental method

X-RAY DIFFRACTION (2.5 Å)