1jm6
From Proteopedia
Pyruvate dehydrogenase kinase, isozyme 2, containing ADP
Overview
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.
About this Structure
1JM6 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of pyruvate dehydrogenase kinase. Novel folding pattern for a serine protein kinase., Steussy CN, Popov KM, Bowker-Kinley MM, Sloan RB Jr, Harris RA, Hamilton JA, J Biol Chem. 2001 Oct 5;276(40):37443-50. Epub 2001 Aug 1. PMID:11483605 Page seeded by OCA on Fri May 2 21:23:45 2008
