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Publication Abstract from PubMed
X-ray structures of the universal translation initiation factor IF2/eIF5B have been determined in three states: free enzyme, inactive IF2/eIF5B.GDP, and active IF2/eIF5B.GTP. The "chalice-shaped" enzyme is a GTPase that facilitates ribosomal subunit joining and Met-tRNA(i) binding to ribosomes in all three kingdoms of life. The conserved core of IF2/eIF5B consists of an N-terminal G domain (I) plus an EF-Tu-type beta barrel (II), followed by a novel alpha/beta/alpha-sandwich (III) connected via an alpha helix to a second EF-Tu-type beta barrel (IV). Structural comparisons reveal a molecular lever, which amplifies a modest conformational change in the Switch 2 region of the G domain induced by Mg(2+)/GTP binding over a distance of 90 A from the G domain active center to domain IV. Mechanisms of GTPase function and ribosome binding are discussed.
X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding.,Roll-Mecak A, Cao C, Dever TE, Burley SK Cell. 2000 Nov 22;103(5):781-92. PMID:11114334[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Roll-Mecak A, Cao C, Dever TE, Burley SK. X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding. Cell. 2000 Nov 22;103(5):781-92. PMID:11114334
