2iea
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E. coli pyruvate dehydrogenase
OverviewOverview
The crystal structure of the recombinant thiamin diphosphate-dependent E1, component from the Escherichia coli pyruvate dehydrogenase multienzyme, complex (PDHc) has been determined at a resolution of 1.85 A. The E. coli, PDHc E1 component E1p is a homodimeric enzyme and crystallizes with an, intact dimer in an asymmetric unit. Each E1p subunit consists of three, domains: N-terminal, middle, and C-terminal, with all having alpha/beta, folds. The functional dimer contains two catalytic centers located at the, interface between subunits. The ThDP cofactors are bound in the "V", conformation in clefts between the two subunits (binding involves the, N-terminal and middle domains), and there is a common ThDP binding fold., The cofactors are completely buried, as only the C2 atoms are accessible, from solution through the active site clefts. Significant structural, differences are observed between individual domains of E1p relative to, heterotetrameric multienzyme complex E1 components operating on branched, chain substrates. These differences may be responsible for reported, alternative E1p binding modes to E2 components within the respective, complexes. This paper represents the first structural example of a, functional pyruvate dehydrogenase E1p component from any species. It also, provides the first representative example for the entire family of, homodimeric (alpha2) E1 multienzyme complex components, and should serve, as a model for this class of enzymes.
About this StructureAbout this Structure
2IEA is a Single protein structure of sequence from Escherichia coli with MG and TDP as ligands. Active as Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution., Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W, Biochemistry. 2002 Apr 23;41(16):5213-21. PMID:11955070
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