Novel Binding Motif and New Flexibility Revealed by Structural Analyses of a Pyruvate Dehydrogenase-Dihydrolipoyl Acetyltransferase Subcomplex from the Escherichia coli Pyruvate Dehydrogenase Multienzyme Complex-Reference-Cited by-同舟云学术

Novel Binding Motif and New Flexibility Revealed by Structural Analyses of a Pyruvate Dehydrogenase-Dihydrolipoyl Acetyltransferase Subcomplex from the Escherichia coli Pyruvate Dehydrogenase Multienzyme Complex

Published:2014-10 Issue:43 Volume:289 Page:30161-30176
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Arjunan Palaniappa,Wang Junjie,Nemeria Natalia S.,Reynolds Shelley,Brown Ian,Chandrasekhar Krishnamoorthy,Calero Guillermo,Jordan Frank,Furey William

Funder

National Institutes of Health

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

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5. The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component;Stephens;Eur. J. Biochem,1983

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