Lu sandbox 1: Difference between revisions
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{{STRUCTURE_1l8a | PDB=1l8a | SCENE= }}Pyruvate dehydrogenase (E1) is one of three main components of the multienzyme complex pyruvate dehydrogenase. It accompanies dihydrolipoyl transacetylase (E2) and dihydrolipoyl dehydrogenase (E3) in comprising this multienzyme complex. Together, these enzymes are responsible for synthesizing acetyl-CoA from pyruvate just prior to entrance into the citric acid cycle. | |||
{{STRUCTURE_1l8a | PDB=1l8a | SCENE= }}Pyruvate dehydrogenase (E1) is one of three main components of the multienzyme complex pyruvate dehydrogenase. It accompanies dihydrolipoyl transacetylase (E2) and dihydrolipoyl dehydrogenase (E3) in comprising this multienzyme complex. Together, these enzymes are responsible for synthesizing acetyl-CoA from pyruvate just prior to entrance into the | |||
==Structure== | ==Structure== | ||
The E. coli enzyme complex has a weight of approximately 4600-kD and a diameter of about 300 angstroms. 24 of the 60 subunits within the complex are E1 proteins. Pyruvate dehydrogenase (E1) falls within the class of alpha and beta proteins<ref>Protein: Pyruvate dehydrogenase E1-beta, PdhB, C-terminal domain from Bacillus stearothermophilus. (2009). Retrieved from http://scop.mrc-lmb.cam.ac.uk</ref>, containing <scene name='Kenny_Coggins_Sandbox_1/Secondary_structure/1'>both alpha helices and beta sheets</scene>, and its structure in E. coli has been solved to a resolution of 1.85 angstroms. That study found that E1 is a homodimer with a molecular weight of 99474 containing α/β folds and bearing two catalytic sites located at the interface between subunits. Each polypeptide chain of E1 consists of 886 residues<ref name="PMID">PMID:11955070</ref>. The structure shown is the E. coli E1 pyruvate dehydrogenase component, PDB code | The E. coli enzyme complex has a weight of approximately 4600-kD and a diameter of about 300 angstroms. 24 of the 60 subunits within the complex are E1 proteins. Pyruvate dehydrogenase (E1) falls within the class of alpha and beta proteins<ref>Protein: Pyruvate dehydrogenase E1-beta, PdhB, C-terminal domain from Bacillus stearothermophilus. (2009). Retrieved from http://scop.mrc-lmb.cam.ac.uk</ref>, containing <scene name='Kenny_Coggins_Sandbox_1/Secondary_structure/1'>both alpha helices and beta sheets</scene>, and its structure in E. coli has been solved to a resolution of 1.85 angstroms. That study found that E1 is a homodimer with a molecular weight of 99474 containing α/β folds and bearing two catalytic sites located at the interface between subunits. Each polypeptide chain of E1 consists of 886 residues<ref name="PMID">PMID:11955070</ref>. The structure shown is the E. coli E1 pyruvate dehydrogenase component, PDB code | ||