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PROTEIN STRUCTURE REPORT

Crystal structure of an enhancer of rudimentary homolog (ERH) at 2.1 Å resolution

¹ Protein Research Group and ² Genome Exploration Research Group, RIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan
³ RIKEN Harima Institute at SPring-8, Mikazuki, Sayo, Hyogo 679-5148, Japan
⁴ Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo 113-0033, Japan

(RECEIVED March 30, 2005; FINAL REVISION March 30, 2005; ACCEPTED April 1, 2005)

The enhancer of rudimentary gene, e(r), of Drosophila melanogaster encodes an enhancer of rudimentary (ER) protein with functions implicated in pyrimidine biosynthesis and the cell cycle. The ER homolog (ERH) is highly conserved among vertebrates, invertebrates, and plants. Xenopus laevis ERH was reported to be a transcriptional repressor. Here we report the 2.1 Å crystal structure of murine ERH (Protein Data Bank ID 1WZ7), determined by the multiwavelength anomalous dispersion (MAD) method. The monomeric structure of ERH comprises a single domain consisting of three -helices and four -strands, which is a novel fold. In the crystal structure, ERH assumes a dimeric structure, through interactions between the -sheet regions. The formation of an ERH dimer is consistent with the results of analytical ultracentrifugation. The residues at the core region and at the dimer interface are highly conserved, suggesting the conservation of the dimer formation as well as the monomer fold. The long flexible loop (44~53) is also significantly conserved, suggesting that this loop region may be important for the functions of ERH. In addition, the putative phosphorylation sites are located at the start of the 2-strand (Thr18) and at the start of the 1-helix (Ser24), implying that the phosphorylation might cause some structural changes.

Keywords: enhancer of rudimentary homolog (ERH); novel fold; pyrimidine biosynthesis; cell cycle, transcriptional repressor, cell-free protein synthesis; structural genomics

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051484505.

Reprint requests to: Shigeyuki Yokoyama, Protein Research Group, Genomic Sciences Center, RIKEN Yokohama Institute, 1-7- 22, Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan; e-mail: yokoyama{at}biochem.s.u-tokyo.ac.jp; fax:+81-45-503-9195.

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