1l8a: Difference between revisions

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[[Image:1l8a.jpg|left|200px]]
{{Seed}}
[[Image:1l8a.png|left|200px]]


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{{STRUCTURE_1l8a|  PDB=1l8a  |  SCENE=  }}  
{{STRUCTURE_1l8a|  PDB=1l8a  |  SCENE=  }}  


'''E. COLI PYRUVATE DEHYDROGENASE'''
===E. COLI PYRUVATE DEHYDROGENASE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11955070}}


==About this Structure==
==About this Structure==
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[[Category: Pyruvate]]
[[Category: Pyruvate]]
[[Category: Thiamin diphosphate]]
[[Category: Thiamin diphosphate]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:39:30 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:56:01 2008''

Revision as of 08:56, 2 July 2008

File:1l8a.png


Drag the structure with the mouse to rotate
1l8a, resolution 1.85Å (default scene)
Ligands: MG, TDP
Activity: Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



E. COLI PYRUVATE DEHYDROGENASE

Template:ABSTRACT PUBMED 11955070

About this Structure

1L8A 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

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