2g43

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(New page: 200px<br /> <applet load="2g43" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g43, resolution 2.09&Aring;" /> '''Structure of the ZN...)
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<applet load="2g43" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2g43, resolution 2.09&Aring;" />
caption="2g43, resolution 2.09&Aring;" />
'''Structure of the ZNF UBP domain from deubiquitinating enzyme isopeptidase T (IsoT)'''<br />
'''Structure of the ZNF UBP domain from deubiquitinating enzyme isopeptidase T (IsoT)'''<br />
==Overview==
==Overview==
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Ubiquitin binding proteins regulate the stability, function, and/or, localization of ubiquitinated proteins. Here we report the crystal, structures of the zinc-finger ubiquitin binding domain (ZnF UBP) from the, deubiquitinating enzyme isopeptidase T (IsoT, or USP5) alone and in, complex with ubiquitin. Unlike other ubiquitin binding domains, this, domain contains a deep binding pocket where the C-terminal diglycine motif, of ubiquitin is inserted, thus explaining the specificity of IsoT for an, unmodified C terminus on the proximal subunit of polyubiquitin. Mutations, in the domain demonstrate that it is required for optimal catalytic, activation of IsoT. This domain is present in several other protein, families, and the ZnF UBP domain from an E3 ligase also requires the C, terminus of ubiquitin for binding. These data suggest that binding the, ubiquitin C terminus may be necessary for the function of other proteins.
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Ubiquitin binding proteins regulate the stability, function, and/or localization of ubiquitinated proteins. Here we report the crystal structures of the zinc-finger ubiquitin binding domain (ZnF UBP) from the deubiquitinating enzyme isopeptidase T (IsoT, or USP5) alone and in complex with ubiquitin. Unlike other ubiquitin binding domains, this domain contains a deep binding pocket where the C-terminal diglycine motif of ubiquitin is inserted, thus explaining the specificity of IsoT for an unmodified C terminus on the proximal subunit of polyubiquitin. Mutations in the domain demonstrate that it is required for optimal catalytic activation of IsoT. This domain is present in several other protein families, and the ZnF UBP domain from an E3 ligase also requires the C terminus of ubiquitin for binding. These data suggest that binding the ubiquitin C terminus may be necessary for the function of other proteins.
==About this Structure==
==About this Structure==
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2G43 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and UNX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2G43 OCA].
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2G43 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=UNX:'>UNX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G43 OCA].
==Reference==
==Reference==
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[[Category: Cheng, X.]]
[[Category: Cheng, X.]]
[[Category: Heroux, A.]]
[[Category: Heroux, A.]]
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[[Category: Horton, J.R.]]
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[[Category: Horton, J R.]]
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[[Category: Mullally, J.E.]]
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[[Category: Mullally, J E.]]
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[[Category: Reyes-Turcu, F.E.]]
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[[Category: Reyes-Turcu, F E.]]
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[[Category: Wilkinson, K.D.]]
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[[Category: Wilkinson, K D.]]
[[Category: UNX]]
[[Category: UNX]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:14:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:54 2008''

Revision as of 15:27, 21 February 2008


2g43, resolution 2.09Å

Drag the structure with the mouse to rotate

Structure of the ZNF UBP domain from deubiquitinating enzyme isopeptidase T (IsoT)

Overview

Ubiquitin binding proteins regulate the stability, function, and/or localization of ubiquitinated proteins. Here we report the crystal structures of the zinc-finger ubiquitin binding domain (ZnF UBP) from the deubiquitinating enzyme isopeptidase T (IsoT, or USP5) alone and in complex with ubiquitin. Unlike other ubiquitin binding domains, this domain contains a deep binding pocket where the C-terminal diglycine motif of ubiquitin is inserted, thus explaining the specificity of IsoT for an unmodified C terminus on the proximal subunit of polyubiquitin. Mutations in the domain demonstrate that it is required for optimal catalytic activation of IsoT. This domain is present in several other protein families, and the ZnF UBP domain from an E3 ligase also requires the C terminus of ubiquitin for binding. These data suggest that binding the ubiquitin C terminus may be necessary for the function of other proteins.

About this Structure

2G43 is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Ubiquitin thiolesterase, with EC number 3.1.2.15 Full crystallographic information is available from OCA.

Reference

The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin., Reyes-Turcu FE, Horton JR, Mullally JE, Heroux A, Cheng X, Wilkinson KD, Cell. 2006 Mar 24;124(6):1197-208. PMID:16564012

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