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Titolo:
PROTEIN-BIOSYNTHESIS - STRUCTURAL STUDIES OF THE ELONGATION CYCLE
Autore:
NYBORG J; LILJAS A;
Indirizzi:
AARHUS UNIV,DEPT MOL & STRUCT BIOL,GUSTAV WIEDS VEJ 10C DK-8000 AARHUS C DENMARK LUND UNIV,DEPT MOL BIOPHYS,CTR CHEM & CHEM ENGN S-22100 LUND SWEDEN
Titolo Testata:
FEBS letters
fascicolo: 1-2, volume: 430, anno: 1998,
pagine: 95 - 99
SICI:
0014-5793(1998)430:1-2<95:P-SSOT>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
FACTOR-EF-TU; AMINOACYL-TRANSFER-RNA; ESCHERICHIA-COLI RIBOSOME; CRYSTAL-STRUCTURE; TERNARY COMPLEX; ANGSTROM RESOLUTION; CHAIN ELONGATION; EFFECTOR REGION; GTP HYDROLYSIS; MECHANISM;
Keywords:
PROTEIN SYNTHESIS; STRUCTURAL ANALYSIS; ELONGATION FACTOR; CRYSTALLOGRAPHY; ELECTRON CRYOMICROSCOPY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
J. Nyborg e A. Liljas, "PROTEIN-BIOSYNTHESIS - STRUCTURAL STUDIES OF THE ELONGATION CYCLE", FEBS letters, 430(1-2), 1998, pp. 95-99

Abstract

The elongation cycle of protein synthesis on ribosomes is catalyzed by the elongation factors EF-Tu and EF-G, A thorough crystallographic analysis of the structures of the different functional states of EF-Tu has been made. Furthermore, the structure of EF-G:GDP is the form of EF-G that dissociates from the ribosome, Since it mimics the structure of the ternary complex of EF-Tu:CTP with aminoacyl-tRNA, which subsequently binds to the ribosome, EF-G:GDP leaves an imprint on the ribosome for the ternary complex. In addition, electron cryomicroscopy studies of ribosomes with tRNA as well as the ternary complex bound are beginning to give a solid structural basis for the functional description of elongation. (C) 1998 Federation of European Biochemical Societies.

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Documento generato il 14/07/20 alle ore 18:50:28