1wz7
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Crystal structure of enhancer of rudimentary homologue (ERH)
OverviewOverview
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, Angstroms 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, alpha-helices and four beta-strands, which is a novel fold. In the crystal, structure, ERH assumes a dimeric structure, through interactions between, the beta-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 approximately 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 beta2-strand (Thr18) and at the start of the alpha1-helix, (Ser24), implying that the phosphorylation might cause some structural, changes.
About this StructureAbout this Structure
1WZ7 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of an enhancer of rudimentary homolog (ERH) at 2.1 Angstroms resolution., Arai R, Kukimoto-Niino M, Uda-Tochio H, Morita S, Uchikubo-Kamo T, Akasaka R, Etou Y, Hayashizaki Y, Kigawa T, Terada T, Shirouzu M, Yokoyama S, Protein Sci. 2005 Jul;14(7):1888-93. Epub 2005 Jun 3. PMID:15937287
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