2ylm

Mechanism of USP7 (HAUSP) activation by its C-terminal ubiquitin-like domain (HUBL) and allosteric regulation by GMP-synthetase.Mechanism of USP7 (HAUSP) activation by its C-terminal ubiquitin-like domain (HUBL) and allosteric regulation by GMP-synthetase.

Structural highlights 2ylm is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 2f1z, 2f1y, 1nbf, 2f1w, 2foj, 1nb8, 2fop, 2f1x, 2foo, 2xxn Activity: Ubiquitinyl hydrolase 1, with EC number 3.4.19.12 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The ubiquitin-specific protease USP7/HAUSP regulates p53 and MDM2 levels, and cellular localization of FOXO4 and PTEN, and hence is critically important for their role in cellular processes. Here we show how the 64 kDa C-terminal region of USP7 can positively regulate deubiquitinating activity. We present the crystal structure of this USP7/HAUSP ubiquitin-like domain (HUBL) comprised of five ubiquitin-like (Ubl) domains organized in 2-1-2 Ubl units. The last di-Ubl unit, HUBL-45, is sufficient to activate USP7, through binding to a "switching" loop in the catalytic domain, which promotes ubiquitin binding and increases activity 100-fold. This activation can be enhanced allosterically by the metabolic enzyme GMPS. It binds to the first three Ubl domains (HUBL-123) and hyperactivates USP7 by stabilization of the HUBL-45-dependent active state. Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase.,Faesen AC, Dirac AM, Shanmugham A, Ovaa H, Perrakis A, Sixma TK Mol Cell. 2011 Oct 7;44(1):147-59. PMID:21981925 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioesterase

spinqualitylabelsall models 2ylm, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image