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- W2140655362 abstract "As part of a structural genomics project, we have determined the 2.0 Å structure of the E1β subunit of pyruvate dehydrogenase from Pyrobaculum aerophilum (PA), a thermophilic archaeon. The overall fold of E1β from PA is closely similar to the previously determined E1β structures from humans (HU) and P. putida (PP). However, unlike the HU and PP structures, the PA structure was determined in the absence of its partner subunit, E1α. Significant structural rearrangements occur in E1β when its E1α partner is absent, including rearrangement of several secondary structure elements such as helix C. Helix C is buried by E1α in the HU and PP structures, but makes crystal contacts in the PA structure that lead to an apparent β4 tetramer. Static light scattering and sedimentation velocity data are consistent with the formation of PA E1β tetramers in solution. The interaction of helix C with its symmetry-related counterpart stabilizes the tetrameric interface, where two glycine residues on the same face of one helix create a packing surface for the other helix. This GΦXXG helix−helix interaction motif has previously been found in interacting transmembrane helices, and is found here at the E1α−E1β interface for both the HU and PP α2β2 tetramers. As a case study in structural genomics, this work illustrates that comparative analysis of protein structures can identify the structural significance of a sequence motif." @default.
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- W2140655362 date "2001-11-08" @default.
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- W2140655362 title "3D Structure and Significance of the GΦXXG Helix Packing Motif in Tetramers of the E1β Subunit of Pyruvate Dehydrogenase from the Archeon <i>Pyrobaculum aerophilum</i><sup>,</sup>" @default.
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- W2140655362 doi "https://doi.org/10.1021/bi011016k" @default.
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