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J. Biol. Chem., Vol. 279, Issue 11, 10634-10642, March 12, 2004

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X-ray Structure of Translation Initiation Factor eIF2

IMPLICATIONS FOR tRNA AND eIF2 BINDING^*

Antonina Roll-Mecak, Pankaj Alone¶, Chune Cao¶, Thomas E. Dever¶, and Stephen K. Burley||**

From the Laboratories of Molecular Biophysics and ^||Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021 and the ^¶Laboratory of Gene Regulation and Development, NICHD, National Institutes of Health, Bethesda, Maryland 20892

The x-ray structure of the -subunit of the heterotrimeric translation initiation factor eIF2 has been determined to 2.4-Å resolution. eIF2 is a GTPase that delivers the initiator Met-tRNA to the P site on the small ribosomal subunit during a rate-limiting initiation step in translation. The structure of eIF2 closely resembles that of EF1A·GTP, consisting of an N-terminal G domain followed by two -barrels arranged in a closed configuration with domain II packed against the G domain in the vicinity of the Switch regions. The G domain of eIF2 has an unusual zinc ribbon motif, not previously found in other GTPases. Structure-based site-directed mutagenesis was used to identify two adjacent features on the surface of eIF2 that bind the -subunit and , respectively. These structural, biochemical, and genetic results provide new insights into eIF2 ternary complex assembly.

Received for publication, September 22, 2003 , and in revised form, December 18, 2003.

The atomic coordinates and structure factors (code 1S0U) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by National Institutes of Health Grant GM61262 (to S. K. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a Burroughs-Wellcome Fund Interfaces training grant to The Rockefeller University.

^** To whom correspondence should be addressed: Structural GenomiX, Inc., 10505 Roselle St., San Diego, CA 92121. Tel.: 858-558-1463; Fax: 858-558-6079; E-mail: stephen_burley{at}stromix.com.

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