Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution.

@article{Arjunan2002StructureOT,
  title={Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution.},
  author={Palaniappa Arjunan and Natalia S. Nemeria and Andrew P J Brunskill and Krishnamoorthy Chandrasekhar and Martin Sax and Yan Yan and Frank Jordan and J. R. Guest and William Furey},
  journal={Biochemistry},
  year={2002},
  volume={41 16},
  pages={5213-21}
}
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… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 23 extracted citations

Similar Papers

Loading similar papers…