2nml
From Proteopedia
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Crystal structure of HEF2/ERH at 1.55 A resolution
Overview
Functional complementation screens can identify known or novel proteins, with important intracellular activities. We have isolated human enhancer, of filamentation 2 (HEF2) in a screen to find human genes that promote, pseudohyphal growth in budding yeast. HEF2 is identical to enhancer of, rudimentary homolog (ERH), a highly conserved protein of 104 amino acids., In silico protein-interaction mapping implies that HEF2/ERH interacts with, transcription factors, cell-cycle regulators, and other proteins shown to, enhance filamentous growth in S. cerevisiae, suggesting a context for, studies of HEF2/ERH function. To provide a mechanistic basis to study of, HEF2/ERH, we have determined the crystal structure of HEF2/ERH at 1.55 A., The crystal asymmetric unit contains a HEF2/ERH monomer. The two monomers, of the physiological dimer are related by the y, x, -z crystal symmetric, operation. The HEF2/ERH structure is characterized by a novel alpha + beta, fold, a four-strand antiparallel beta-sheet with three alpha-helixes on, one side of the sheet. The beta-sheets from the two monomers together, constitute a pseudo-beta-barrel, and form the center of the functional, HEF2/ERH dimer, with a cavity channel at the dimer interface. Docking of, this structure to the HEF2/ERH partner protein DCOH/PCD suggests that, HEF2/ERH may regulate the oligomeric state of this protein. These data, suggest that HEF2/ERH may be an important transcription regulator that, also functions in the control of cell-cycle progression.
About this Structure
2NML is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 2I4F. Full crystallographic information is available from OCA.
Reference
A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks., Jin T, Guo F, Serebriiskii IG, Howard A, Zhang YZ, Proteins. 2007 Aug 1;68(2):427-37. PMID:17444515
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