4z4k

Crystal structure of GFP-TAX1BP1 UBZ1+2 domain fusion protein

spinqualitylabelsall models 4z4k, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4z4k is a 2 chain structure with sequence from Aequorea victoria and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CR2, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TAXB1_HUMAN Inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. Degraded by caspase-3-like family proteins upon TNF-induced apoptosis. May also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. Publication Abstract from PubMed The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating beta-beta-alpha fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. Here we report the crystal structure of the UBZ domain of Y-family DNA polymerase (pol) eta and the crystal structure of the complex between the UBZ domain of Werner helicase-interacting protein 1 (WRNIP1) and ubiquitin, crystallized using the green fluorescent protein fusion technique. In contrast to the pol eta UBZ, which has been proposed to bind ubiquitin via its C-terminal alpha helix, ubiquitin binds to a novel surface of WRNIP1 UBZ composed of the first beta strand and the C-terminal alpha helix. In addition, we report the structure of the tandem UBZ domains of Tax1-binding protein 1 (TAX1BP1) and show that the second UBZ of TAX1BP1 binds ubiquitin, presumably in a manner similar to that of WRNIP1 UBZ. We propose that UBZ domains can be divided into at least two different types in terms of the ubiquitin-binding surfaces: the pol eta type and the WRNIP1 type. This article is protected by copyright. All rights reserved. A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1.,Suzuki N, Rohaim A, Kato R, Dikic I, Wakatsuki S, Kawasaki M FEBS J. 2016 Apr 8. doi: 10.1111/febs.13734. PMID:27062441 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Green Fluorescent Protein 3D structures

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