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| CRYSTAL-STRUCTURE OF ACTIVE ELONGATION-FACTOR TU REVEALS MAJOR DOMAIN REARRANGEMENTS |
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| Author(s): BERCHTOLD H, RESHETNIKOVA L, REISER COA, SCHIRMER NK, SPRINZL M, HILGENFELD R |
| Source: NATURE Volume: 365 Issue: 6442 Pages: 126-132 Published: SEP 9 1993 |
| Times Cited: 423 References: 50 |
| Abstract: 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 angstrom, with incorporation of data extending to 1.45 angstrom. The effector region, including interaction sites for the ribosome and for transfer RNA, is well defined. Molecular mechanisms are proposed for transduction 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 rearrangements of the three domains of the molecule. |
| Document Type: Article |
| Language: English |
Addresses:
1. HOECHST AKT GESELL, CENT RES G865A, PROT CRYSTALLOG, D-65926 FRANKFURT, GERMANY
2. UNIV BAYREUTH, BIOCHEM LAB, D-95440 BAYREUTH, GERMANY
3. VA ENGELHARDT MOLEC BIOL INST, MOSCOW 117984, RUSSIA |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: LW442 |
| ISSN: 0028-0836 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |