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2dok

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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: unknown function]]
[[Category: unknown function]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:19:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:01 2008''

Revision as of 15:01, 21 February 2008

Image:2dok.jpg

2dok, resolution 1.80Å

Drag the structure with the mouse to rotate

Crystal structure of the PIN domain of human EST1A

Overview

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.

About this Structure

2DOK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the PIN domain of human telomerase-associated protein EST1A., Takeshita D, Zenno S, Lee WC, Saigo K, Tanokura M, Proteins. 2007 Sep 1;68(4):980-9. PMID:17557331

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