2g3q: Difference between revisions

Revision as of 14:40, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2g3q.png

Template:STRUCTURE 2g3q

Solution Structure of Ede1 UBA-ubiquitin complexSolution Structure of Ede1 UBA-ubiquitin complex

Template:ABSTRACT PUBMED 16563434

About this StructureAbout this Structure

2G3Q is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full experimental information is available from OCA.

ReferenceReference

Structural basis for monoubiquitin recognition by the Ede1 UBA domain., Swanson KA, Hicke L, Radhakrishnan I, J Mol Biol. 2006 May 5;358(3):713-24. Epub 2006 Mar 9. PMID:16563434

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-'''Solution Structure of Ede1 UBA-ubiquitin complex'''
+===Solution Structure of Ede1 UBA-ubiquitin complex===
-==Overview==
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-Monoubiquitination is a general mechanism for downregulating the activity of cell surface receptors by consigning these proteins for lysosome-mediated degradation through the endocytic pathway. The yeast Ede1 protein functions at the internalization step of endocytosis and binds monoubiquitinated proteins through a ubiquitin associated (UBA) domain. UBA domains are found in a broad range of cellular proteins but previous studies have suggested that the mode of ubiquitin recognition might not be universally conserved. Here we present the solution structure of the Ede1 UBA domain in complex with monoubiquitin. The Ede1 UBA domain forms a three-helix bundle structure and binds ubiquitin through a largely hydrophobic surface in a manner reminiscent of the Dsk2 UBA and the remotely homologous Cue2 CUE domains, for which high-resolution structures have been described. However, the interaction is dissimilar to the molecular models proposed for the hHR23A UBA domains bound to either monoubiquitin or Lys48-linked diubiquitin. Our mutational analyses of the Ede1 UBA domain-ubiquitin interaction reveal several key affinity determinants and, unexpectedly, a negative affinity determinant in the wild-type Ede1 protein, implying that high-affinity interactions may not be the sole criterion for optimal function of monoubiquitin-binding endocytic proteins.
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+{{ABSTRACT_PUBMED_16563434}}
 ==About this Structure==
-G3Q is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G3Q OCA].
+G3Q is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G3Q OCA].
 ==Reference==
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 [[Category: Uba domain]]
 [[Category: Ubiquitin-binding motif]]
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