2bwb
From Proteopedia
(New page: 200px<br /><applet load="2bwb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bwb, resolution 2.30Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:2bwb.gif|left|200px]]<br /><applet load="2bwb" size=" | + | [[Image:2bwb.gif|left|200px]]<br /><applet load="2bwb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bwb, resolution 2.30Å" /> | caption="2bwb, resolution 2.30Å" /> | ||
'''CRYSTAL STRUCTURE OF THE UBA DOMAIN OF DSK2 FROM S. CEREVISIAE'''<br /> | '''CRYSTAL STRUCTURE OF THE UBA DOMAIN OF DSK2 FROM S. CEREVISIAE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The yeast proteins Dsk2 and Rad23 belong to a family of proteins that | + | The yeast proteins Dsk2 and Rad23 belong to a family of proteins that contain an N-terminal ubiquitin-like domain (UBL) and a C-terminal ubiquitin-associated domain (UBA). Both Dsk2 and Rad23 function as adaptors to target ubiquitin-labelled proteins to the proteasome through recognition of polyubiquitin (four or more K48-linked ubiquitins) by their UBA domains and to the yeast proteasomal subunit Rpn1 by their UBL domains. The crystal structures of the Dsk2 UBL domain, the Dsk2 UBA domain and the Dsk2 UBA-UBL complex are reported. In the crystal, the Dsk2 UBA domains associate through electrostatic interactions to form ninefold helical ribbons that leave the ubiquitin-binding surface exposed. The UBA-UBL complex explains the reduced affinity of the UBA domain for UBL compared with ubiquitin and has implications for the regulation of Dsk2 adaptor function during ubiquitin-mediated proteasomal targeting. A model is discussed in which two or more Dsk2 UBA molecules may selectively bind to K48-linked polyubiquitin. |
==About this Structure== | ==About this Structure== | ||
| - | 2BWB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 2BWB is a [http://en.wikipedia.org/wiki/Single_protein 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=2BWB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brown, N | + | [[Category: Brown, N R.]] |
| - | [[Category: Endicott, J | + | [[Category: Endicott, J A.]] |
[[Category: Fonso, L.]] | [[Category: Fonso, L.]] | ||
[[Category: Hasan, N.]] | [[Category: Hasan, N.]] | ||
| - | [[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: signaling protein]] | [[Category: signaling protein]] | ||
[[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 16:42:21 2008'' |
Revision as of 14:42, 21 February 2008
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CRYSTAL STRUCTURE OF THE UBA DOMAIN OF DSK2 FROM S. CEREVISIAE
Overview
The yeast proteins Dsk2 and Rad23 belong to a family of proteins that contain an N-terminal ubiquitin-like domain (UBL) and a C-terminal ubiquitin-associated domain (UBA). Both Dsk2 and Rad23 function as adaptors to target ubiquitin-labelled proteins to the proteasome through recognition of polyubiquitin (four or more K48-linked ubiquitins) by their UBA domains and to the yeast proteasomal subunit Rpn1 by their UBL domains. The crystal structures of the Dsk2 UBL domain, the Dsk2 UBA domain and the Dsk2 UBA-UBL complex are reported. In the crystal, the Dsk2 UBA domains associate through electrostatic interactions to form ninefold helical ribbons that leave the ubiquitin-binding surface exposed. The UBA-UBL complex explains the reduced affinity of the UBA domain for UBL compared with ubiquitin and has implications for the regulation of Dsk2 adaptor function during ubiquitin-mediated proteasomal targeting. A model is discussed in which two or more Dsk2 UBA molecules may selectively bind to K48-linked polyubiquitin.
About this Structure
2BWB is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structures of the Dsk2 UBL and UBA domains and their complex., Lowe ED, Hasan N, Trempe JF, Fonso L, Noble ME, Endicott JA, Johnson LN, Brown NR, Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):177-88. Epub 2006, Jan 18. PMID:16421449
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