Crystal structure of active elongation factor Tu reveals major domain rearrangements.
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 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.
Berchtold
H
H
Central Research G 865A, Hoechst Aktiengesellschaft, Frankfurt, Germany.
Reshetnikova
L
L
Reiser
C O
CO
Schirmer
N K
NK
Sprinzl
M
M
Hilgenfeld
R
R
D003196:Computer Graphics; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000378:metabolism; D008274:Magnesium / Q000737:chemistry; D008958:Models, Molecular; D009711:Nucleotides / Q000378:metabolism; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D016963:Thermus thermophilus / Q000737:chemistry; D014961:X-Ray Diffraction
D009711:Nucleotides; D020963:GTP Phosphohydrolase-Linked Elongation Factors; D010444:Peptide Elongation Factor Tu; D008274:Magnesium