1yx4

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(New page: 200px<br /> <applet load="1yx4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yx4" /> '''Structure of S5a bound to monoubiquitin pro...)
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'''Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition'''<br />
'''Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition'''<br />
==Overview==
==Overview==
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Ubiquitin is a key regulatory molecule in diverse cellular events. How, cells determine the outcome of ubiquitylation remains unclear; however, a, likely determinant is the specificity of ubiquitin receptor proteins for, polyubiquitin chains of certain length and linkage. Proteasome subunit S5a, contains two ubiquitin-interacting motifs (UIMs) through which it recruits, ubiquitylated substrates to the proteasome for their degradation. Here, we, report the structure of S5a (196-306) alone and complexed with two, monoubiquitin molecules. This construct contains the two UIMs of S5a and, we reveal their different ubiquitin-binding mechanisms and provide a, rationale for their unique specificities for different ubiquitin-like, domains. Furthermore, we provide direct evidence that S5a (196-306) binds, either K63-linked or K48-linked polyubiquitin, and in both cases prefers, longer chains. On the basis of these results we present a model for how, S5a and other ubiquitin-binding proteins recognize polyubiquitin.
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Ubiquitin is a key regulatory molecule in diverse cellular events. How cells determine the outcome of ubiquitylation remains unclear; however, a likely determinant is the specificity of ubiquitin receptor proteins for polyubiquitin chains of certain length and linkage. Proteasome subunit S5a contains two ubiquitin-interacting motifs (UIMs) through which it recruits ubiquitylated substrates to the proteasome for their degradation. Here, we report the structure of S5a (196-306) alone and complexed with two monoubiquitin molecules. This construct contains the two UIMs of S5a and we reveal their different ubiquitin-binding mechanisms and provide a rationale for their unique specificities for different ubiquitin-like domains. Furthermore, we provide direct evidence that S5a (196-306) binds either K63-linked or K48-linked polyubiquitin, and in both cases prefers longer chains. On the basis of these results we present a model for how S5a and other ubiquitin-binding proteins recognize polyubiquitin.
==About this Structure==
==About this Structure==
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1YX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YX4 OCA].
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1YX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX4 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Walters, K.J.]]
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[[Category: Walters, K J.]]
[[Category: Wang, Q.]]
[[Category: Wang, Q.]]
[[Category: Young, P.]]
[[Category: Young, P.]]
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[[Category: uim]]
[[Category: uim]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:26:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:59 2008''

Revision as of 14:10, 21 February 2008

Image:1yx4.gif

1yx4

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Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition

Overview

Ubiquitin is a key regulatory molecule in diverse cellular events. How cells determine the outcome of ubiquitylation remains unclear; however, a likely determinant is the specificity of ubiquitin receptor proteins for polyubiquitin chains of certain length and linkage. Proteasome subunit S5a contains two ubiquitin-interacting motifs (UIMs) through which it recruits ubiquitylated substrates to the proteasome for their degradation. Here, we report the structure of S5a (196-306) alone and complexed with two monoubiquitin molecules. This construct contains the two UIMs of S5a and we reveal their different ubiquitin-binding mechanisms and provide a rationale for their unique specificities for different ubiquitin-like domains. Furthermore, we provide direct evidence that S5a (196-306) binds either K63-linked or K48-linked polyubiquitin, and in both cases prefers longer chains. On the basis of these results we present a model for how S5a and other ubiquitin-binding proteins recognize polyubiquitin.

About this Structure

1YX4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition., Wang Q, Young P, Walters KJ, J Mol Biol. 2005 May 6;348(3):727-39. PMID:15826667

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