1nbf: Difference between revisions

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~~'''~~Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde~~'''~~

===Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde===

~~==Overview==~~

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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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12507430}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12507430 is the PubMed ID number.

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==About this Structure==

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[[Category: Hausp]]

[[Category: Ubiquitin binding]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:19:52 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:39:33 2008''

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-[[Image:1nbf.gif|left|200px]]
+{{Seed}}
+[[Image:1nbf.png|left|200px]]
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 {{STRUCTURE_1nbf|  PDB=1nbf  |  SCENE=  }}
-'''Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde'''
+===Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12507430}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12507430 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12507430}}
 ==About this Structure==
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 [[Category: Hausp]]
 [[Category: Ubiquitin binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:19:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:39:33 2008''