2vc8: Difference between revisions

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[[Image:2vc8.gif|left|200px]]
[[Image:2vc8.gif|left|200px]]


{{Structure
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{{STRUCTURE_2vc8| PDB=2vc8  | SCENE= }}  
|RELATEDENTRY=[[2rm4|2RM4]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vc8 OCA], [http://www.ebi.ac.uk/pdbsum/2vc8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vc8 RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE LSM DOMAIN OF HUMAN EDC3 (ENHANCER OF DECAPPING 3)'''
'''CRYSTAL STRUCTURE OF THE LSM DOMAIN OF HUMAN EDC3 (ENHANCER OF DECAPPING 3)'''
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[[Category: Tritschler, F.]]
[[Category: Tritschler, F.]]
[[Category: Weichenrieder, O.]]
[[Category: Weichenrieder, O.]]
[[Category: cytoplasm]]
[[Category: Cytoplasm]]
[[Category: enhancer of mrna decapping]]
[[Category: Enhancer of mrna decapping]]
[[Category: p-body component]]
[[Category: P-body component]]
[[Category: protein-binding]]
[[Category: Protein-binding]]
[[Category: rna]]
[[Category: Rna]]
[[Category: sm-like protein]]
[[Category: Sm-like protein]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:10:52 2008''

Revision as of 15:34, 4 May 2008

File:2vc8.gif

Template:STRUCTURE 2vc8

CRYSTAL STRUCTURE OF THE LSM DOMAIN OF HUMAN EDC3 (ENHANCER OF DECAPPING 3)


Overview

Members of the (L)Sm (Sm and Sm-like) protein family are found across all kingdoms of life and play crucial roles in RNA metabolism. The P-body component EDC3 (enhancer of decapping 3) is a divergent member of this family that functions in mRNA decapping. EDC3 is composed of a N-terminal LSm domain, a central FDF domain, and a C-terminal YjeF-N domain. We show that this modular architecture enables EDC3 to interact with multiple components of the decapping machinery, including DCP1, DCP2, and Me31B. The LSm domain mediates DCP1 binding and P-body localization. We determined the three-dimensional structures of the LSm domains of Drosophila melanogaster and human EDC3 and show that the domain adopts a divergent Sm fold that lacks the characteristic N-terminal alpha-helix and has a disrupted beta4-strand. This domain remains monomeric in solution and lacks several features that canonical (L)Sm domains require for binding RNA. The structures also revealed a conserved patch of surface residues that are required for the interaction with DCP1 but not for P-body localization. The conservation of surface and of critical structural residues indicates that LSm domains in EDC3 proteins adopt a similar fold that has separable novel functions that are absent in canonical (L)Sm proteins.

About this Structure

2VC8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting., Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O, Mol Cell Biol. 2007 Dec;27(24):8600-11. Epub 2007 Oct 8. PMID:17923697 Page seeded by OCA on Sun May 4 18:34:49 2008

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