2bwe: Difference between revisions

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[[Image:2bwe.gif|left|200px]]<br /><applet load="2bwe" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2bwe.gif|left|200px]]<br /><applet load="2bwe" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2bwe, resolution 3.10Å" />

'''THE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE UBA AND UBL DOMAINS OF DSK2'''<br />

==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.

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==

2BWE 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2BWE OCA].

2BWE 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=2BWE OCA].

==Reference==

Line 13:

[[Category: Saccharomyces cerevisiae]]

[[Category: Single protein]]

[[Category: Brown, N.R.]]

[[Category: Brown, N R.]]

[[Category: Endicott, J.A.]]

[[Category: Endicott, J A.]]

[[Category: Fonso, L.]]

[[Category: Hasan, N.]]

[[Category: Johnson, L.N.]]

[[Category: Johnson, L N.]]

[[Category: Lowe, E.D.]]

[[Category: Lowe, E D.]]

[[Category: Noble, M.E.M.]]

[[Category: Noble, M E.M.]]

[[Category: Trempe, J-F.]]

[[Category: protein/protein interaction]]

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[[Category: ubiquitin-like proteins]]

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@@ Line 1: / Line 1: @@
-[[Image:2bwe.gif|left|200px]]<br /><applet load="2bwe" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2bwe.gif|left|200px]]<br /><applet load="2bwe" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2bwe, resolution 3.10&Aring;" />
 '''THE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE UBA AND UBL DOMAINS OF DSK2'''<br />
 ==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.
+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==
-BWE 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BWE OCA].
+BWE 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=2BWE OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Brown, N.R.]]
+[[Category: Brown, N R.]]
-[[Category: Endicott, J.A.]]
+[[Category: Endicott, J A.]]
 [[Category: Fonso, L.]]
 [[Category: Hasan, N.]]
-[[Category: Johnson, L.N.]]
+[[Category: Johnson, L N.]]
-[[Category: Lowe, E.D.]]
+[[Category: Lowe, E D.]]
-[[Category: Noble, M.E.M.]]
+[[Category: Noble, M E.M.]]
 [[Category: Trempe, J-F.]]
 [[Category: protein/protein interaction]]
@@ Line 26: / Line 26: @@
 [[Category: ubiquitin-like proteins]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:56:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:22 2008''