Structural Studies on the 2.25-MDa Homomultimeric Phosphoenolpyruvate Synthase fromStaphylothermus marinus

The phosphoenolpyruvate synthase of the hyperthermophilic archaeonStaphylothermus marinusforms an unusually large homomultimeric complex of 93 kDa subunits. Electron image analysis of negatively stained and low-dose unstained preparations showed that the complex has a single, stable characteristic v...

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Bibliographic Details
Published in:Journal of structural biology 1996-03, Vol.116 (2), p.290-301
Main Authors: Harauz, George, Cicicopol, Christiana, Hegerl, Reiner, Cejka, Zdenka, Goldie, Kenneth, Santarius, Ute, Engel, Andreas, Baumeister, Wolfgang
Format: Article
Language:English
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Summary:The phosphoenolpyruvate synthase of the hyperthermophilic archaeonStaphylothermus marinusforms an unusually large homomultimeric complex of 93 kDa subunits. Electron image analysis of negatively stained and low-dose unstained preparations showed that the complex has a single, stable characteristic view and a well-preserved core with threefold rotational symmetry. The periphery of the assembly is composed of a nebulous, possibly flexible, component. Mass measurements by scanning transmission electron microscopy yielded a molecular weight of 2250 ± 230 kDa, confirming the well-defined nature of the structure and indicating that it is composed of 24 ± 2.5 subunits. The stability and symmetry of the characteristic projection views suggest a polyhedral three-dimensional architecture. The novel quaternary arrangement of this enzyme might be a consequence of its adaptation to an extreme environment.
ISSN:1047-8477
1095-8657
DOI:10.1006/jsbi.1996.0044