2iea
From Proteopedia
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[[Image:2iea.gif|left|200px]] | [[Image:2iea.gif|left|200px]] | ||
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'''E. coli pyruvate dehydrogenase''' | '''E. coli pyruvate dehydrogenase''' | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11955070 11955070] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11955070 11955070] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Pyruvate dehydrogenase (acetyl-transferring)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Arjunan, P.]] | [[Category: Arjunan, P.]] | ||
[[Category: Furey, W.]] | [[Category: Furey, W.]] | ||
| - | [[Category: | + | [[Category: Alpha-keto acid dehydrogenase]] |
| - | [[Category: | + | [[Category: Pyruvate]] |
| - | [[Category: | + | [[Category: Thiamin diphosphate]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:23:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:23, 4 May 2008
E. coli pyruvate dehydrogenase
Overview
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 Structure
2IEA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 07:23:58 2008
