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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



  history
ID: 318610.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Structural studies on the 2.25-mda homomultimeric phosphoenolpyruvate synthase from staphylothermus marinus
Authors:Harauz, G.; Cicicopol, C.; Hegerl, R.; Cejka, Z.; Goldie, K.; Santarius, U.; Engel, A.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1996
Title of Journal:Journal of Structural Biology
Volume:116
Issue / Number:2
Start Page:290
End Page:301
Review Status:not specified
Audience:Not Specified
Abstract / Description: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]
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.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)
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