1wz7: Difference between revisions

Revision as of 16:33, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1wz7.png

Template:STRUCTURE 1wz7

Crystal structure of enhancer of rudimentary homologue (ERH)Crystal structure of enhancer of rudimentary homologue (ERH)

Template:ABSTRACT PUBMED 15937287

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of enhancer of rudimentary homologue (ERH)'''
+===Crystal structure of enhancer of rudimentary homologue (ERH)===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15937287}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15937287}}
 ==About this Structure==
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 [[Category: Rsgi]]
 [[Category: Structural genomic]]
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