1nb8

From Proteopedia

Revision as of 14:27, 15 February 2008

Structure of the catalytic domain of USP7 (HAUSP)

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

1NB8 is a Single protein structure of sequence 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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