2vfj | pdb_00002vfj

STRUCTURE OF THE A20 OVARIAN TUMOUR (OTU) DOMAIN

File:2vfj.jpg

spinqualitylabelsall models 2vfj, resolution 3.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

Overview

The NF-kappaB (nuclear factor kappaB) regulator A20 antagonises IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). In the present paper we describe the crystal structure of the N-terminal OTU (ovarian tumour) deubiquitinase domain of A20, which differs from other deubiquitinases but shares the minimal catalytic core with otubain-2. Analysis of conserved surface regions allows prediction of ubiquitin-binding sites for the proximal and distal ubiquitin molecules. Structural and biochemical analysis suggests a novel architecture of the catalytic triad, which might be present in a subset of OTU domains including Cezanne and TRABID (TRAF-binding domain). Biochemical analysis shows a preference of the isolated A20 OTU domain for Lys48-linked tetraubiquitin in vitro suggesting that additional specificity factors might be required for the physiological function of A20 in cells.

About this Structure

2VFJ is a Single protein structure of sequence from Homo sapiens with SO4 and MG as ligands. Active as Ubiquitinyl hydrolase 1, with EC number 3.4.19.12 Known structural/functional Sites: AC1, AC2, AC3, AC4 and AC5. Full crystallographic information is available from OCA.

Reference

Structure of the A20 OTU domain and mechanistic insights into deubiquitination., Komander D, Barford D, Biochem J. 2008 Jan 1;409(1):77-85. PMID:17961127

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