2NML

Crystal structure of HEF2/ERH at 1.55 A resolution

「2I4F」から置き換えられました

2NML の概要

• エントリーDOI: 10.2210/pdb2nml/pdb
• 分子名称: Enhancer of rudimentary homolog (2 entities in total)
• 機能のキーワード: hef2/erh fold, pseudo beta barrel, interaction network, transcription, cell cycle
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12273.93

構造登録者

Jin, T.C.,Guo, F.,Serebriiskii, I.G.,Howard, A.J.,Zhang, Y.Z. (登録日: 2006-10-21, 公開日: 2006-10-31, 最終更新日: 2023-12-27)

主引用文献

Jin, T.,Guo, F.,Serebriiskii, I.G.,Howard, A.,Zhang, Y.Z.
A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks.
Proteins, 68:427-437, 2007

PubMed Abstract: 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.

PubMed: 17444515
DOI: 10.1002/prot.21343

実験手法

X-RAY DIFFRACTION (1.55 Å)