1zc1
From Proteopedia
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| - | [[Image:1zc1.gif|left|200px]] | + | [[Image:1zc1.gif|left|200px]] |
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| - | '''Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites''' | + | {{Structure |
| + | |PDB= 1zc1 |SIZE=350|CAPTION= <scene name='initialview01'>1zc1</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= UFD1, PIP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZC1 is a [ | + | 1ZC1 is a [[Single protein]] structure of sequence 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=1ZC1 OCA]. |
==Reference== | ==Reference== | ||
| - | Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites., Park S, Isaacson R, Kim HT, Silver PA, Wagner G, Structure. 2005 Jul;13(7):995-1005. PMID:[http:// | + | Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites., Park S, Isaacson R, Kim HT, Silver PA, Wagner G, Structure. 2005 Jul;13(7):995-1005. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16004872 16004872] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ufd1]] | [[Category: ufd1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:33:42 2008'' |
Revision as of 13:33, 20 March 2008
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| Gene: | UFD1, PIP3 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
Overview
Ufd1 mediates ubiquitin fusion degradation by association with Npl4 and Cdc48/p97. The Ufd1-ubiquitin interaction is essential for transfer of substrates to the proteasome. However, the mechanism and specificity of ubiquitin recognition by Ufd1 are poorly understood due to the lack of detailed structural information. Here, we present the solution structure of yeast Ufd1 N domain and show that it has two distinct binding sites for mono- and polyubiquitin. The structure exhibits striking similarities to the Cdc48/p97 N domain. It contains the double-psi beta barrel motif, which is thus identified as a ubiquitin binding domain. Significantly, Ufd1 shows higher affinity toward polyubiquitin than monoubiquitin, attributable to the utilization of separate binding sites with different affinities. Further studies revealed that the Ufd1-ubiquitin interaction involves hydrophobic contacts similar to those in well-characterized ubiquitin binding proteins. Our results provide a structural basis for a previously proposed synergistic binding of polyubiquitin by Cdc48/p97 and Ufd1.
About this Structure
1ZC1 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites., Park S, Isaacson R, Kim HT, Silver PA, Wagner G, Structure. 2005 Jul;13(7):995-1005. PMID:16004872
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