TY - JOUR
T1 - Crystal structure of active elongation factor Tu reveals major domain rearrangements
AU - Berchtold, Harald
AU - Reshetnikova, Ludmila
AU - Reiser, Christian O.A.
AU - Schirmer, Norbert K.
AU - Sprinzl, Mathias
AU - Hilgenfeld, Rolf
N1 - Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1993
Y1 - 1993
N2 - 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 Å, with incorporation of data extending to 1.45 Å. 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.
AB - 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 Å, with incorporation of data extending to 1.45 Å. 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.
UR - http://www.scopus.com/inward/record.url?scp=0027179878&partnerID=8YFLogxK
U2 - 10.1038/365126a0
DO - 10.1038/365126a0
M3 - Journal articles
C2 - 8371755
AN - SCOPUS:0027179878
SN - 0028-0836
VL - 365
SP - 126
EP - 132
JO - Nature
JF - Nature
IS - 6442
ER -
