2DOK

Crystal structure of the PIN domain of human EST1A

2DOK の概要

• エントリーDOI: 10.2210/pdb2dok/pdb
• 分子名称: Telomerase-binding protein EST1A (2 entities in total)
• 機能のキーワード: telomerase-associated protein, unknown function
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus, nucleolus: Q86US8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42220.47

構造登録者

Takeshita, D. (登録日: 2006-05-01, 公開日: 2007-05-01, 最終更新日: 2024-03-13)

主引用文献

Takeshita, D.,Zenno, S.,Lee, W.C.,Saigo, K.,Tanokura, M.
Crystal structure of the PIN domain of human telomerase-associated protein EST1A
Proteins, 68:980-989, 2007

PubMed Abstract: Saccharomyces cerevisiae Est1p is a telomerase-associated protein essential for telomere length homeostasis. hEST1A is one of the three human Est1p homologues and is considered to be involved not only in regulation of telomere elongation or capping but also in nonsense-mediated degradation of RNA. hEST1A is composed of two conserved regions, Est1p homology and PIN (PilT N-terminus) domains. The present study shows the crystal structure of the PIN domain at 1.8 A resolution. The overall structure is composed of an alpha/beta fold or a core structure similar to the counterpart of 5' nucleases and an extended structure absent from archaeal PIN-domain proteins and 5' nucleases. The structural properties of the PIN domain indicate its putative active center consisting of invariant acidic amino acid residues, which is geometrically similar to the active center of 5' nucleases and an archaeal PAE2754 PIN-domain protein associated with exonuclease activity.

PubMed: 17557331
DOI: 10.1002/prot.21351

実験手法

X-RAY DIFFRACTION (1.8 Å)