First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
1w9g
From Proteopedia
| 1w9g, resolution 2.00Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Domains: | ER | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
STRUCTURE OF ERH (ENHENCER OF RUDIMENTARY GENE)
erh (enhancer of rudimentary homolog) is a ubiquitously expressed transcriptional coregulator that is highly conserved among eukaryotes, from humans to plants to protozoa. Functions attributed to erh include enhancement of pyrimidine biosynthesis, a role in cell cycle regulation, and repression of the tissue-specific transcription factor HNF-1 (hepatocyte nuclear factor-1) through binding the coactivator DCoH (dimerization cofactor of HNF1). No homologous sequences, other than erh orthologs, have been identified, and little is known about the interactions of erh. To further elucidate its function, we determined the crystal structure of erh to 2.0 A resolution. The erh structure is a novel alpha + beta fold consisting of a four-stranded antiparallel beta sheet with three amphipathic alpha helices situated on one face of the beta sheet. Structure-based searches of the Protein Data Bank, like sequence-based searches, failed to identify paralogs. We present structural and biochemical evidence that erh functions as a dimer. The dimer interface consists of a beta sandwich composed of the beta sheet from each monomer. Many of the surface residues of erh are conserved, including patches of hydrophobic and charged residues, suggesting protein-protein interaction interfaces. Two putative CKII phosphorylation sites are highly ordered in the structure and are predicted to disrupt dimerization and protein-protein interactions.
Structure of the conserved transcriptional repressor enhancer of rudimentary homolog., Wan C, Tempel W, Liu ZJ, Wang BC, Rose RB, Biochemistry. 2005 Apr 5;44(13):5017-23. PMID:15794639
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1W9G is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Wan C, Tempel W, Liu ZJ, Wang BC, Rose RB. Structure of the conserved transcriptional repressor enhancer of rudimentary homolog. Biochemistry. 2005 Apr 5;44(13):5017-23. PMID:15794639 doi:10.1021/bi047785w
Page seeded by OCA on Tue Feb 17 03:05:37 2009
Categories: Homo sapiens | Liu, Z. | Rose, R B. | Tempel, W. | Wan, C. | Wang, B C.

