Structural studies on the 2.25-mda homomultimeric phosphoenolpyruvate synthase 
from staphylothermus marinus

Harauz, G.; Cicicopol, C.; Hegerl, R.; Cejka, Z.; Goldie, K.; Santarius, U.; Engel, A.; Baumeister, W.

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Structural studies on the 2.25-mda homomultimeric phosphoenolpyruvate synthase from staphylothermus marinus

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Harauz, G., Cicicopol, C., Hegerl, R., Cejka, Z., Goldie, K., Santarius, U., et al. (1996). Structural studies on the 2.25-mda homomultimeric phosphoenolpyruvate synthase from staphylothermus marinus. Journal of Structural Biology, 116(2), 290-301.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-731B-9

Abstract

The phosphoenolpyruvate synthase of the hyperthermophilic archaeon Staphylothermus marinus forms 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. (C) 1996 Academic Press, Inc. [References: 72]