1jm6
From Proteopedia
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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 with and as ligands. Active as [Pyruvate_dehydrogenase_(acetyl-transferring)_kinase [Pyruvate dehydrogenase (acetyl-transferring)] kinase], with EC number 2.7.11.2 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[[Category: [Pyruvate dehydrogenase (acetyl-transferring)] kinase]]
Page seeded by OCA on Thu Feb 21 13:24:11 2008
