Abstract
The 2-oxo acid dehydrogenase multienzyme complexes are among the best examples of multifunctional proteins fashioned from independently-folded protein domains joined by linker sequences of various lengths and degrees of conformational flexibility (Patel and Roche, 1990; Perham, 1991). The structural core of these complexes is provided by the dihydrolipoyl acyltransferase (E2) component, an aggregate of 24 or 60 polypeptide chains arranged with octahedral or icosahedral symmetry, respectively, according to the source. The E2 chains themselves are highly segmented: they comprise, from the N-terminus, up to three lipoyl domains, a peripheral subunit-binding domain, and a large core-forming acyltransferase domain, all linked together by long (25–30 residue) segments of polypeptide chain rich in alanine, proline and charged/hydrophilic amino acids (Reed and Hackert, 1990; Perham, 1991).
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References
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Perham, R.N., Wallis, N.G., Brocklehurst, S.M., Dardel, F., Davis, A.L., Laue, E.D. (1993). Structure and Post-Translational Modification of the Lipoyl Domain of 2-Oxo Acid Dehydrogenase Complexes: A New Family of Protein Domains. In: Imahori, K., Sakiyama, F. (eds) Methods in Protein Sequence Analysis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1603-7_37
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DOI: https://doi.org/10.1007/978-1-4899-1603-7_37
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