2bwf
From Proteopedia
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==Overview== | ==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 .. | + | 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== | ||
| - | 2BWF is a | + | 2BWF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with FMT as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BWF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:58:57 2007'' |
Revision as of 10:53, 5 November 2007
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CRYSTAL STURCTURE OF THE UBL 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
2BWF is a Single protein structure of sequence from Saccharomyces cerevisiae with FMT as ligand. Structure known Active Site: AC1. 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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