1nbf
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1nbf.gif|left|200px]] | [[Image:1nbf.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1nbf", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{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''' | ||
Line 35: | Line 32: | ||
[[Category: Wu, J W.]] | [[Category: Wu, J W.]] | ||
[[Category: Yao, T.]] | [[Category: Yao, T.]] | ||
- | [[Category: | + | [[Category: Catalytic mechanisms of upb]] |
- | [[Category: | + | [[Category: Deubiquitinating enzyme]] |
- | [[Category: | + | [[Category: Hausp]] |
- | [[Category: | + | [[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 | + |
Revision as of 23:19, 2 May 2008
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.
About this Structure
1NBF is a Protein complex structure of sequences from Homo sapiens. 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 Page seeded by OCA on Sat May 3 02:19:52 2008