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  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., et al. (1996). Structural studies on the 2.25-mda homomultimeric phosphoenolpyruvate synthase from staphylothermus marinus. Journal of Structural Biology, 116(2), 290-301.

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Harauz, G., Author
Cicicopol, C., Author
Hegerl, R.1, Author              
Cejka, Z., Author
Goldie, K., Author
Santarius, U.1, Author              
Engel, A., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Sugar phosphotransferase system; Transmission electron-microscopy; Heavy riboflavin synthase; Escherichia-coli; Enzyme-i; Bacterial phosphoenolpyruvate; Single particles; Image-analysis; 3-dimensional reconstruction; Thermophilic archaebacterium.; Cell & developmental biology.
 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]

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 Dates: 1996
 Publication Status: Published in print
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 Identifiers: eDoc: 318610
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Title: Journal of Structural Biology
Source Genre: Journal
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Pages: - Volume / Issue: 116 (2) Sequence Number: - Start / End Page: 290 - 301 Identifier: -