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Published December 2005 | public
Journal Article

Electron Cryotomography of the E. coli Pyruvate and 2-Oxoglutarate Dehydrogenase Complexes

Abstract

The E. coli pyruvate and 2-oxoglutarate dehydrogenases are two closely related, large complexes that exemplify a growing number of multiprotein "machines" whose domains have been studied extensively and modeled in atomic detail, but whose quaternary structures have remained unclear for lack of an effective imaging technology. Here, electron cryotomography was used to show that the E1 and E3 subunits of these complexes are flexibly tethered ~11 nm away from the E2 core. This result demonstrates unambiguously that electron cryotomography can reveal the relative positions of features as small as 80 kDa in individual complexes, elucidating quaternary structure and conformational flexibility.

Additional Information

© 2005 Elsevier. Received 27 May 2005; revised 27 July 2005; accepted 1 August 2005. Published: December 13, 2005. Available online 13 December 2005. We thank T. Wagenknecht and J. Berkowitz for the protein samples and A. Rawlinson for help preparing the figures. This work was supported in part by National Institutes of Health Grant PO1 GM66521 to G.J.J., Department of Energy grant DE-FG02-04ER63785 to G.J.J., the Beckman Institute at Caltech, and gifts to Caltech from the Ralph M. Parsons Foundation, the Agouron Institute, and the Gordon and Betty Moore Foundation. Accession Numbers: One extracted PDHC particle and one OGDHC particle were submitted to the EM Data Bank with the accession codes EMD-1151 and EMD-1152, respectively.

Additional details

Created:
August 19, 2023
Modified:
October 23, 2023