1uoc
From Proteopedia
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|PDB= 1uoc |SIZE=350|CAPTION= <scene name='initialview01'>1uoc</scene>, resolution 2.30Å | |PDB= 1uoc |SIZE=350|CAPTION= <scene name='initialview01'>1uoc</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=AC1:Environment+For+Xe+In+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Environment+For+Xe+In+Chain+B'>AC1</scene> | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=XE:XENON'>XE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uoc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uoc OCA], [http://www.ebi.ac.uk/pdbsum/1uoc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uoc RCSB]</span> | ||
}} | }} | ||
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[[Category: Suck, D.]] | [[Category: Suck, D.]] | ||
[[Category: Thore, S.]] | [[Category: Thore, S.]] | ||
- | [[Category: CA]] | ||
- | [[Category: XE]] | ||
[[Category: dedd nuclease]] | [[Category: dedd nuclease]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:13:03 2008'' |
Revision as of 21:13, 30 March 2008
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, resolution 2.30Å | |||||||
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Sites: | |||||||
Ligands: | , | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
X-RAY STRUCTURE OF THE RNASE DOMAIN OF THE YEAST POP2 PROTEIN
Overview
In Saccharomyces cerevisiae, a large complex, known as the Ccr4-Not complex, containing two nucleases, is responsible for mRNA deadenylation. One of these nucleases is called Pop2 and has been identified by similarity with PARN, a human poly(A) nuclease. Here, we present the crystal structure of the nuclease domain of Pop2 at 2.3 A resolution. The domain has the fold of the DnaQ family and represents the first structure of an RNase from the DEDD superfamily. Despite the presence of two non-canonical residues in the active site, the domain displays RNase activity on a broad range of RNA substrates. Site-directed mutagenesis of active-site residues demonstrates the intrinsic ability of the Pop2 RNase D domain to digest RNA. This first structure of a nuclease involved in the 3'-5' deadenylation of mRNA in yeast provides information for the understanding of the mechanism by which the Ccr4-Not complex achieves its functions.
About this Structure
1UOC is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex., Thore S, Mauxion F, Seraphin B, Suck D, EMBO Rep. 2003 Dec;4(12):1150-5. Epub 2003 Nov 14. PMID:14618157
Page seeded by OCA on Mon Mar 31 00:13:03 2008