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2p51

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{{STRUCTURE_2p51| PDB=2p51 | SCENE= }}
{{STRUCTURE_2p51| PDB=2p51 | SCENE= }}
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'''Crystal structure of the S. pombe Pop2p deadenylation subunit'''
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===Crystal structure of the S. pombe Pop2p deadenylation subunit===
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==Overview==
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Deadenylation is the first and probably also rate-limiting step of controlled mRNA decay in eukaryotes and therefore central for the overall rate of gene expression. In yeast, the process is maintained by the mega-Dalton Ccr4-Not complex, of which both the Ccr4p and Pop2p subunits are 3'-5' exonucleases potentially responsible for the deadenylation reaction. Here, we present the crystal structure of the Pop2p subunit from Schizosaccharomyces pombe determined to 1.4 A resolution and show that the enzyme is a competent ribonuclease with a tunable specificity towards poly-A. In contrast to S. cerevisiae Pop2p, the S. pombe enzyme contains a fully conserved DEDDh active site, and the high resolution allows for a detailed analysis of its configuration, including divalent metal ion binding. Functional data further indicates that the identity of the ions in the active site can modulate both activity and specificity of the enzyme, and finally structural superposition of single nucleotides and poly-A oligonucleotides provide insight into the catalytic cycle of the protein.
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{{ABSTRACT_PUBMED_17452359}}
==About this Structure==
==About this Structure==
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[[Category: Van, L B.]]
[[Category: Van, L B.]]
[[Category: Dedd nuclease fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:22:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:20:48 2008''

Revision as of 06:20, 28 July 2008

Image:2p51.png

Template:STRUCTURE 2p51

Crystal structure of the S. pombe Pop2p deadenylation subunit

Template:ABSTRACT PUBMED 17452359

About this Structure

2P51 is a Single protein structure of sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.

Reference

The 1.4-A crystal structure of the S. pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme., Jonstrup AT, Andersen KR, Van LB, Brodersen DE, Nucleic Acids Res. 2007;35(9):3153-64. Epub 2007 Apr 22. PMID:17452359

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