1Z7L
Crystal structure of fragment of mouse ubiquitin-activating enzyme
Summary for 1Z7L
| Entry DOI | 10.2210/pdb1z7l/pdb |
| Descriptor | Ubiquitin-activating enzyme E1 1, HEXATANTALUM DODECABROMIDE (2 entities in total) |
| Functional Keywords | scch, ubiquitin-activating enzyme, second catalytic cysteine half-domain, ligase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 3 |
| Total formula weight | 100124.23 |
| Authors | Szczepanowski, R.H.,Filipek, R.,Bochtler, M. (deposition date: 2005-03-25, release date: 2005-04-12, Last modification date: 2024-02-14) |
| Primary citation | Szczepanowski, R.H.,Filipek, R.,Bochtler, M. Crystal structure of a fragment of mouse ubiquitin-activating enzyme. J.Biol.Chem., 280:22006-22011, 2005 Cited by PubMed Abstract: Protein ubiquitination requires the sequential activity of three enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin-ligase (E3). The ubiquitin-transfer machinery is hierarchically organized; for every ubiquitin-activating enzyme, there are several ubiquitin-conjugating enzymes, and most ubiquitin-conjugating enzymes can in turn interact with multiple ubiquitin ligases. Despite the central role of ubiquitin-activating enzyme in this cascade, a crystal structure of a ubiquitin-activating enzyme is not available. The enzyme is thought to consist of an adenylation domain, a catalytic cysteine domain, a four-helix bundle, and possibly, a ubiquitin-like domain. Its adenylation domain can be modeled because it is clearly homologous to the structurally known adenylation domains of the activating enzymes for the small ubiquitin-like modifier (SUMO) and for the protein encoded by the neuronal precursor cell-expressed, developmentally down-regulated gene 8 (NEDD8). Low sequence similarity and vastly different domain lengths make modeling difficult for the catalytic cysteine domain that results from the juxtaposition of two catalytic cysteine half-domains. Here, we present a biochemical and crystallographic characterization of the two half-domains and the crystal structure of the larger, second catalytic cysteine half-domain of mouse ubiquitin-activating enzyme. We show that the domain is organized around a conserved folding motif that is also present in the NEDD8- and SUMO-activating enzymes, and we propose a tentative model for full-length ubiquitin-activating enzyme. PubMed: 15774460DOI: 10.1074/jbc.M502583200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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