1L8A

E. COLI PYRUVATE DEHYDROGENASE

Summary for 1L8A

• Entry DOI: 10.2210/pdb1l8a/pdb
• Descriptor: Pyruvate dehydrogenase E1 component, MAGNESIUM ION, THIAMINE DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: thiamin diphosphate, pyruvate, alpha-keto acid dehydrogenase, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 200213.57

Authors

Furey, W.,Arjunan, P. (deposition date: 2002-03-19, release date: 2002-07-24, Last modification date: 2024-02-14)

Primary citation

Arjunan, P.,Nemeria, N.,Brunskill, A.,Chandrasekhar, K.,Sax, M.,Yan, Y.,Jordan, F.,Guest, J.R.,Furey, W.
Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution.
Biochemistry, 41:5213-5221, 2002

PubMed Abstract: 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.

PubMed: 11955070
DOI: 10.1021/bi0118557

Experimental method

X-RAY DIFFRACTION (1.85 Å)