Literature summary for 2.7.11.2 extracted from

Devedjiev, Y.; Steussy, C.N.; Vassylyev, D.G.
Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications (2007), J. Mol. Biol., 370, 407-416.

Crystallization (Commentary)

Crystallization (Comment)	Organism
isozyme PDHK3 in an asymmetric complex with L2, hanging-drop vapor diffusion technique, mixing of 0.002 ml of protein solution containing 3-5 mg/ml of the PDHK3/L2 complex, 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 5 mM DTT, and 2.5% v/v ethylene glycol with an equal volume of reservoir solution containing 100 mM histidine, pH 6.4, 30 mM EDTA, and 7% v/v 2,4-methyl penthane diol, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement, modelling	Homo sapiens

Crystallization (Comment)

Organism

isozyme PDHK3 in an asymmetric complex with L2, hanging-drop vapor diffusion technique, mixing of 0.002 ml of protein solution containing 3-5 mg/ml of the PDHK3/L2 complex, 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 5 mM DTT, and 2.5% v/v ethylene glycol with an equal volume of reservoir solution containing 100 mM histidine, pH 6.4, 30 mM EDTA, and 7% v/v 2,4-methyl penthane diol, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement, modelling

Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	a homodimer of pyruvate dehydrogenase kinase is an integral part of the pyruvate dehydrogenase complex, PDC, to which it is anchore primarily through the inner lipoyl-bearing domains L2 of transacetylase component, binding structure, catalytic cycle of PDHK and its translocation over the PDC surface is thought to be mediated by the symmetric and asymmetric modes, in which the PDHK dimer binds to two and one L2-domain(s), respectively, overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	isozyme PDK3	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	a homodimer of pyruvate dehydrogenase kinase is an integral part of the pyruvate dehydrogenase complex, PDC, to which it is anchore primarily through the inner lipoyl-bearing domains L2 of transacetylase component, binding structure, catalytic cycle of PDHK and its translocation over the PDC surface is thought to be mediated by the symmetric and asymmetric modes, in which the PDHK dimer binds to two and one L2-domain(s), respectively, overview	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	a homodimer of pyruvate dehydrogenase kinase is an integral part of the pyruvate dehydrogenase complex, PDC, to which it is anchore primarily through the inner lipoyl-bearing domains L2 of transacetylase component, the PDHK3 subunits have distinct conformations: one subunit exhibits open and the other closed configuration of the putative substrate-binding cleft, domain organization, binding structure, modeling, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
PDHK	-	Homo sapiens
pyruvate dehydrogenase kinase	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	the ATP-binding loop in one PDHK3 subunit adopts an open conformation, implying that the nucleotide loading into the active site is mediated by the inactive pre-insertion binding mode	Homo sapiens