1WZ7

Crystal structure of enhancer of rudimentary homologue (ERH)

Summary for 1WZ7

• Entry DOI: 10.2210/pdb1wz7/pdb
• Descriptor: Enhancer of rudimentary homolog (2 entities in total)
• Functional Keywords: alpha/beta, structural genomics, riken structural genomics/proteomics initiative, rsgi, transcription
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 3
• Total formula weight: 39105.18

Authors

Arai, R.,Kukimoto-Niino, M.,Uda-Tochio, H.,Morita, S.,Uchikubo-Kamo, T.,Kigawa, T.,Terada, T.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-02-26, release date: 2005-05-03, Last modification date: 2024-10-30)

Primary citation

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.
Crystal structure of an enhancer of rudimentary homolog (ERH) at 2.1 Angstroms resolution.
Protein Sci., 14:1888-1893, 2005

PubMed Abstract: 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.

PubMed: 15937287
DOI: 10.1110/ps.051484505

Experimental method

X-RAY DIFFRACTION (2.1 Å)