2g45
From Proteopedia
(New page: 200px<br /> <applet load="2g45" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g45, resolution 1.99Å" /> '''Co-crystal structur...) |
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| - | [[Image:2g45.gif|left|200px]]<br /> | + | [[Image:2g45.gif|left|200px]]<br /><applet load="2g45" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2g45" size=" | + | |
caption="2g45, resolution 1.99Å" /> | caption="2g45, resolution 1.99Å" /> | ||
'''Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin'''<br /> | '''Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ubiquitin binding proteins regulate the stability, function, and/or | + | 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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| + | ==Disease== | ||
| + | Known disease associated with this structure: Cleft palate, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191339 191339]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2G45 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and CL 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:// | + | 2G45 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CL:'>CL</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=2G45 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cheng, X.]] | [[Category: Cheng, X.]] | ||
[[Category: Heroux, A.]] | [[Category: Heroux, A.]] | ||
| - | [[Category: Horton, J | + | [[Category: Horton, J R.]] |
| - | [[Category: Mullally, J | + | [[Category: Mullally, J E.]] |
| - | [[Category: Reyes-Turcu, F | + | [[Category: Reyes-Turcu, F E.]] |
| - | [[Category: Wilkinson, K | + | [[Category: Wilkinson, K D.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:53 2008'' |
Revision as of 15:27, 21 February 2008
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Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin
Contents |
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.
Disease
Known disease associated with this structure: Cleft palate, isolated OMIM:[191339]
About this Structure
2G45 is a Protein complex structure of sequences 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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