Structural Studies on the 2.25-MDa Homomultimeric Phosphoenolpyruvate Synthase fromStaphylothermus marinus
| Autor: | Reiner Hegerl, Christiana Cicicopol, George Harauz, Wolfgang Baumeister, Zdenka Cejka, Kenneth N. Goldie, Andreas Engel, Ute Santarius |
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| Rok vydání: | 1996 |
| Předmět: |
Microscopy
Electron Scanning Transmission chemistry.chemical_classification Hot Temperature Protein Conformation Phosphoenolpyruvate synthase Heavy riboflavin synthase Biology medicine.disease_cause Archaea Evolution Molecular Molecular Weight Phosphotransferases (Paired Acceptors) Enzyme Bacterial Proteins Biochemistry chemistry Multienzyme Complexes Structural Biology Transmission electron microscopy Staphylothermus marinus Scanning transmission electron microscopy Image Processing Computer-Assisted medicine Extreme environment Escherichia coli |
| Zdroj: | Journal of Structural Biology. 116:290-301 |
| ISSN: | 1047-8477 |
| DOI: | 10.1006/jsbi.1996.0044 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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