2DOK

Crystal structure of the PIN domain of human EST1A

Summary for 2DOK

• Entry DOI: 10.2210/pdb2dok/pdb
• Descriptor: Telomerase-binding protein EST1A (2 entities in total)
• Functional Keywords: telomerase-associated protein, unknown function
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus, nucleolus: Q86US8
• Total number of polymer chains: 2
• Total formula weight: 42220.47

Authors

Takeshita, D. (deposition date: 2006-05-01, release date: 2007-05-01, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)