Crystal structure of active elongation factor Tu reveals major domain rearrangements
| Autor: | Harald Berchtold, Christian O. A. Reiser, Rolf Hilgenfeld, Ludmila Reshetnikova, Mathias Sprinzl, Norbert K. Schirmer |
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| Rok vydání: | 1993 |
| Předmět: |
Models
Molecular Multidisciplinary biology GTP' Nucleotides Protein Conformation Stereochemistry Effector Thermus thermophilus GTPase Peptide Elongation Factor Tu biology.organism_classification Ribosome X-Ray Diffraction GTP Phosphohydrolase-Linked Elongation Factors Transfer RNA Computer Graphics Magnesium EF-Ts EF-Tu |
| Zdroj: | Nature. 365:126-132 |
| ISSN: | 1476-4687 0028-0836 |
| Popis: | The crystal structure of intact elongation factor Tu (EF-Tu) from Thermus thermophilus has been determined and refined at an effective resolution of 1.7 A, with incorporation of data extending to 1.45 A. The effector region, including interaction sites for the ribosome and for transfer RNA, is well defined. Molecular mechanisms are proposed for transductlon and amplification of the signal induced by GTP binding as well as for the intrinsic and effector-enhanced GTPase activity of EF-Tu. Comparison of the structure with that of EF-Tu–GDP reveals major mutual rearrange-ments of the three domains of the molecule. |
| Databáze: | OpenAIRE |
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