1nbf
From Proteopedia
(New page: 200px<br /> <applet load="1nbf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nbf, resolution 2.3Å" /> '''Crystal structure of...) |
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| - | [[Image:1nbf.gif|left|200px]]<br /> | + | [[Image:1nbf.gif|left|200px]]<br /><applet load="1nbf" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1nbf, resolution 2.3Å" /> | caption="1nbf, resolution 2.3Å" /> | ||
'''Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde'''<br /> | '''Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ubiquitin-specific processing protease (UBP) family of | + | The ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an essential role in numerous cellular processes. HAUSP, a representative UBP, specifically deubiquitinates and hence stabilizes the tumor suppressor protein p53. Here, we report the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin aldehyde. These studies reveal that the UBP deubiquitinating enzymes exhibit a conserved three-domain architecture, comprising Fingers, Palm, and Thumb. The leaving ubiquitin moiety is specifically coordinated by the Fingers, with its C terminus placed in the active site between the Palm and the Thumb. Binding by ubiquitin aldehyde induces a drastic conformational change in the active site that realigns the catalytic triad residues for catalysis. |
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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== | ||
| - | 1NBF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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:// | + | 1NBF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1NBF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ubiquitin thiolesterase]] | [[Category: Ubiquitin thiolesterase]] | ||
| - | [[Category: Cohen, R | + | [[Category: Cohen, R E.]] |
[[Category: Gu, W.]] | [[Category: Gu, W.]] | ||
[[Category: Hu, M.]] | [[Category: Hu, M.]] | ||
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[[Category: Li, W.]] | [[Category: Li, W.]] | ||
[[Category: Shi, Y.]] | [[Category: Shi, Y.]] | ||
| - | [[Category: Wu, J | + | [[Category: Wu, J W.]] |
[[Category: Yao, T.]] | [[Category: Yao, T.]] | ||
[[Category: catalytic mechanisms of upbs]] | [[Category: catalytic mechanisms of upbs]] | ||
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[[Category: ubiquitin binding]] | [[Category: ubiquitin binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:15 2008'' |
Revision as of 12:04, 21 February 2008
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Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
Contents |
Overview
The ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an essential role in numerous cellular processes. HAUSP, a representative UBP, specifically deubiquitinates and hence stabilizes the tumor suppressor protein p53. Here, we report the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin aldehyde. These studies reveal that the UBP deubiquitinating enzymes exhibit a conserved three-domain architecture, comprising Fingers, Palm, and Thumb. The leaving ubiquitin moiety is specifically coordinated by the Fingers, with its C terminus placed in the active site between the Palm and the Thumb. Binding by ubiquitin aldehyde induces a drastic conformational change in the active site that realigns the catalytic triad residues for catalysis.
Disease
Known disease associated with this structure: Cleft palate, isolated OMIM:[191339]
About this Structure
1NBF is a Protein complex structure of sequences from Homo sapiens. Active as Ubiquitin thiolesterase, with EC number 3.1.2.15 Full crystallographic information is available from OCA.
Reference
Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde., Hu M, Li P, Li M, Li W, Yao T, Wu JW, Gu W, Cohen RE, Shi Y, Cell. 2002 Dec 27;111(7):1041-54. PMID:12507430
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