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On The Unique Structural Organization of the Saccharomyces Cerevisiae Pyruvate Dehydrogenase Complex

Published online by Cambridge University Press:  02 July 2020

James K. Stoops ,
Z. Hong Zhou ,
John P. Schroeter ,
Steven J. Kolodziej ,
R. Holland Cheng ,
Timothy S. Baker ,
Diane L. B. McCarthy ,
Mohammed A. Yazdi ,
Cheol-Young Maeng  and
Lester J. Reed
James K. Stoops
Affiliation:
Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, 6431 Fannin Street, Houston, TX77030
Z. Hong Zhou
Affiliation:
Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, 6431 Fannin Street, Houston, TX77030
John P. Schroeter
Affiliation:
Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, 6431 Fannin Street, Houston, TX77030
Steven J. Kolodziej
Affiliation:
Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, 6431 Fannin Street, Houston, TX77030
R. Holland Cheng
Affiliation:
Department of Bioscience, Novum Center for Biotechnology, Karolinska Institute, S-141 57, Huddinge, Sweden
Timothy S. Baker
Affiliation:
Department of Biological Sciences, Purdue University, West Lafayette, IN47907
Diane L. B. McCarthy
Affiliation:
Biochemical Institute and Department of Chemistry and Biochemistry, The University of Texas, Austin, TX78712
Mohammed A. Yazdi
Affiliation:
Biochemical Institute and Department of Chemistry and Biochemistry, The University of Texas, Austin, TX78712
Cheol-Young Maeng
Affiliation:
Biochemical Institute and Department of Chemistry and Biochemistry, The University of Texas, Austin, TX78712
Lester J. Reed
Affiliation:
Biochemical Institute and Department of Chemistry and Biochemistry, The University of Texas, Austin, TX78712
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Extract

Dihydrohpoamide acetyl transferase (E2), a catalytic and structural component of a multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate, forms the central core to which the other components are bound. We have utilized protein engineering and 3-D electron microscopy to study the structural organization of the largest multienzyme complex known (Mr ∼ 107). The structures of the truncated 60-mer core (tE2) and complexes of the tE2 associated with a binding protein (BP), and the BP associated with its dihydrohpoamide dehydrogenase (BP'E3) and the intact E2 associated with BP and the pyruvate dehydrogenase (E1) were determined (Figs. 1 and 2). The tE2 core is a pentagonal dodecahedron consisting of 20 cone-shaped trimers interconnected by 30 bridges.

Previous studies have given rise to the generally accepted belief that BP and BP'E3 components are bound on the outside of the E2 scaffold and that E1 is similarly bound to the core in variable positions by flexible tethers.

Type
Imaging of Macromolecular Complexes
Information
Microscopy and Microanalysis , Volume 4 , Issue S2: Proceedings: Microscopy & Microanalysis '98, Microscopy Society of America 56th Annual Meeting, Microbeam Analysis Society 32nd Annual Meeting, Atlanta, Georgia July 12-16, 1998 , July 1998 , pp. 954 - 955
Copyright
Copyright © Microscopy Society of America

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