1ukx

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Solution structure of the RWD domain of mouse GCN2

Overview

GCN2 is the alpha-subunit of the only translation initiation factor, (eIF2alpha) kinase that appears in all eukaryotes. Its function requires, an interaction with GCN1 via the domain at its N-terminus, which is termed, the RWD domain after three major RWD-containing proteins: RING, finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD, (DEXD)-like helicases. In this study, we determined the solution structure, of the mouse GCN2 RWD domain using NMR spectroscopy. The structure forms, an alpha + beta sandwich fold consisting of two layers: a four-stranded, antiparallel beta-sheet, and three side-by-side alpha-helices, with an, alphabetabetabetabetaalphaalpha topology. A characteristic YPXXXP motif, which always occurs in RWD domains, forms a stable loop including three, consecutive beta-turns that overlap with each other by two residues, (triple beta-turn). As putative binding sites with GCN1, a structure-based, alignment allowed the identification of several surface residues in, alpha-helix 3 that are characteristic of the GCN2 RWD domains. Despite the, apparent absence of sequence similarity, the RWD structure significantly, resembles that of ubiquitin-conjugating enzymes (E2s), with most of the, structural differences in the region connecting beta-strand 4 and, alpha-helix 3. The structural architecture, including the triple, beta-turn, is fundamentally common among various RWD domains and E2s, but, most of the surface residues on the structure vary. Thus, it appears that, the RWD domain is a novel structural domain for protein-binding that plays, specific roles in individual RWD-containing proteins.

About this Structure

1UKX is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Solution structure of the RWD domain of the mouse GCN2 protein., Nameki N, Yoneyama M, Koshiba S, Tochio N, Inoue M, Seki E, Matsuda T, Tomo Y, Harada T, Saito K, Kobayashi N, Yabuki T, Aoki M, Nunokawa E, Matsuda N, Sakagami N, Terada T, Shirouzu M, Yoshida M, Hirota H, Osanai T, Tanaka A, Arakawa T, Carninci P, Kawai J, Hayashizaki Y, Kinoshita K, Guntert P, Kigawa T, Yokoyama S, Protein Sci. 2004 Aug;13(8):2089-100. PMID:15273307

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