Lu sandbox 1: Difference between revisions

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==Structure==

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'>mixed alpha helices and beta sheets</scene>. It is a multimeric protein. Mammalian E1s, including human E1, are heterotetrameric, composed of two α- and two β- subunits<ref>Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS (June 2003). "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase". J. Biol. Chem. 278 (23): 21240–6</ref>. E1 from E. coli is, however, a homodimer with a molecular weight of 99474 containing α/β folds. It has 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

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'>mixed alpha helices and beta sheets</scene>. It is a multimeric protein. Mammalian E1s, including human E1, are heterotetrameric, composed of two α- and two β- subunits<ref>Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS (June 2003). "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase". J. Biol. Chem. 278 (23): 21240–6</ref>. E1 from E. coli is, however, a homodimer with a molecular weight of 99474 containing α/β folds. It has two catalytic sites located at the interface between subunits. Each polypeptide chain consists of 886 residues<ref name="PMID">PMID:11955070</ref>. The structure shown is the E. coli E1 pyruvate dehydrogenase component, PDB code

[[1l8a]]<ref>Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/</ref>.

Lu sandbox 1: Difference between revisions

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 ==Structure==
-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'>mixed alpha helices and beta sheets</scene>. It is a multimeric protein. Mammalian E1s, including human E1, are heterotetrameric, composed of two α- and two β- subunits<ref>Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS (June 2003). "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase". J. Biol. Chem. 278 (23): 21240–6</ref>. E1 from E. coli is, however, a homodimer with a molecular weight of 99474 containing α/β folds. It has 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
+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'>mixed alpha helices and beta sheets</scene>. It is a multimeric protein. Mammalian E1s, including human E1, are heterotetrameric, composed of two α- and two β- subunits<ref>Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS (June 2003). "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase". J. Biol. Chem. 278 (23): 21240–6</ref>. E1 from E. coli is, however, a homodimer with a molecular weight of 99474 containing α/β folds. It has two catalytic sites located at the interface between subunits.  Each polypeptide chain consists of 886 residues<ref name="PMID">PMID:11955070</ref>.  The structure shown is the E. coli E1 pyruvate dehydrogenase component, PDB code
 [[1l8a]]<ref>Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/</ref>.