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X‐ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha‐helix.
Author(s) -
Biou V.,
Shu F.,
Ramakrishnan V.
Publication year - 1995
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1995.tb00077.x
Subject(s) - national laboratory , physics , library science , biology , engineering physics , computer science
The structures of the two domains of translational initiation factor IF3 from Bacillus stearothermophilus have been solved by X‐ray crystallography using single wavelength anomalous scattering and multiwavelength anomalous diffraction. Each of the two domains has an alpha/beta topology, with an exposed beta‐sheet that is reminiscent of several ribosomal and other RNA binding proteins. An alpha‐helix that protrudes out from the body of the N‐terminal domain towards the C‐terminal domain suggests that IF3 consists of two RNA binding domains connected by an alpha‐helix and that it may bridge two regions of the ribosome. This represents the first high resolution structural information on a translational initiation factor.