1z96
From Proteopedia
(New page: 200px<br /><applet load="1z96" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z96, resolution 1.80Å" /> '''Crystal structure of...) |
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| - | [[Image:1z96.gif|left|200px]]<br /><applet load="1z96" size=" | + | [[Image:1z96.gif|left|200px]]<br /><applet load="1z96" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z96, resolution 1.80Å" /> | caption="1z96, resolution 1.80Å" /> | ||
'''Crystal structure of the Mud1 UBA domain'''<br /> | '''Crystal structure of the Mud1 UBA domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ubiquitin-pathway associated (UBA) domain is a 40-residue | + | The ubiquitin-pathway associated (UBA) domain is a 40-residue polyubiquitin-binding motif. The Schizosaccharomyces pombe protein Mud1 is an ortholog of the Saccharomyces cerevisiae DNA-damage response protein Ddi1 and binds to K48-linked polyubiquitin through its UBA domain. We have solved the crystal structure of Mud1 UBA at 1.8 angstroms resolution, revealing a canonical three-helical UBA fold. We have probed the interactions of this domain using mutagenesis, surface plasmon resonance, NMR and analytical ultracentrifugation. We show that the ubiquitin-binding surface of Mud1 UBA extends beyond previously recognized motifs and can be functionally dissected into primary and secondary ubiquitin-binding sites. Mutation of Phe330 to alanine, a residue exposed between helices 2 and 3, significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyubiquitin, despite leaving the primary binding surface functionally intact. Moreover, K48-linked diubiquitin binds a single Mud1 UBA domain even in the presence of excess UBA. We therefore propose a mechanism for the recognition of K48-linked polyubiquitin chains by Mud1 in which diubiquitin units are specifically recognized by a single UBA domain. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z96 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http:// | + | 1Z96 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z96 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Schizosaccharomyces pombe]] | [[Category: Schizosaccharomyces pombe]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brown, N | + | [[Category: Brown, N R.]] |
| - | [[Category: Campbell, I | + | [[Category: Campbell, I D.]] |
| - | [[Category: Endicott, J | + | [[Category: Endicott, J A.]] |
[[Category: Gordon, C.]] | [[Category: Gordon, C.]] | ||
| - | [[Category: Johnson, L | + | [[Category: Johnson, L N.]] |
| - | [[Category: Lowe, E | + | [[Category: Lowe, E D.]] |
| - | [[Category: Noble, M | + | [[Category: Noble, M E.M.]] |
| - | [[Category: Trempe, J | + | [[Category: Trempe, J F.]] |
[[Category: three-helix bundle]] | [[Category: three-helix bundle]] | ||
[[Category: uba]] | [[Category: uba]] | ||
[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:18 2008'' |
Revision as of 14:13, 21 February 2008
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Crystal structure of the Mud1 UBA domain
Overview
The ubiquitin-pathway associated (UBA) domain is a 40-residue polyubiquitin-binding motif. The Schizosaccharomyces pombe protein Mud1 is an ortholog of the Saccharomyces cerevisiae DNA-damage response protein Ddi1 and binds to K48-linked polyubiquitin through its UBA domain. We have solved the crystal structure of Mud1 UBA at 1.8 angstroms resolution, revealing a canonical three-helical UBA fold. We have probed the interactions of this domain using mutagenesis, surface plasmon resonance, NMR and analytical ultracentrifugation. We show that the ubiquitin-binding surface of Mud1 UBA extends beyond previously recognized motifs and can be functionally dissected into primary and secondary ubiquitin-binding sites. Mutation of Phe330 to alanine, a residue exposed between helices 2 and 3, significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyubiquitin, despite leaving the primary binding surface functionally intact. Moreover, K48-linked diubiquitin binds a single Mud1 UBA domain even in the presence of excess UBA. We therefore propose a mechanism for the recognition of K48-linked polyubiquitin chains by Mud1 in which diubiquitin units are specifically recognized by a single UBA domain.
About this Structure
1Z96 is a Single protein structure of sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.
Reference
Mechanism of Lys48-linked polyubiquitin chain recognition by the Mud1 UBA domain., Trempe JF, Brown NR, Lowe ED, Gordon C, Campbell ID, Noble ME, Endicott JA, EMBO J. 2005 Sep 21;24(18):3178-89. Epub 2005 Sep 1. PMID:16138082
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