Bayer, Peter and Arndt, Andreas and Metzger, Susanne and Mahajan, Rohit and Melchior, Frauke and Jaenicke, Rainer and Becker, Jörg (1998) Structure determination of the small ubiquitin-related modifier SUMO-1. JOURNAL OF MOLECULAR BIOLOGY, 280 (2). pp. 275-286. ISSN 0022-2836, 1089-8638
Full text not available from this repository.Abstract
The recently discovered small ubiquitin-related modifier SUMO-1 belongs to the growing family of ubiquitin-related proteins involved in postranslational protein modification. Unlike ubiquitin, SUMO-1 does not appear to target proteins for degradation but seems to be involved in the modulation of protein-protein interactions. Independent studies demonstrate an essential function of SUMO-1 in the regulation of nucleo-cytoplasmic transport, and suggest a role in cell-cycle regulation and apoptosis. Here, we present the first three-dimensional structure of SUMO-1 solved by NMR. Although having only 18% amino acid sequence identity with ubiquitin, the overall structure closely resembles that of ubiquitin, featuring the beta beta alpha beta alpha beta fold of the ubiquitin protein family. In addition, the position of the two C-terminal Gly residues required for isopeptide bond formation is conserved between ubiquitin and SUMO-1. The most prominent feature of SUMO-1 is a long and highly flexible N terminus, which protrudes from the core of the protein and which is absent in ubiquitin. Furthermore, ubiquitin Lys48, required to generate ubiquitin polymers, is substituted in SUMO-1 by Gln69 at the same position, which provides an explanation of why SUMO-1 has not been observed to form polymers. Moreover, the hydrophobic core of SUMO-1 and ubiquitin is maintained by conserved hydrophobic residues, whereas the overall charge topology of SUMO-1 and ubiquitin differs significantly, suggesting specific modifying enzymes and target proteins for both proteins. (C) 1998 Academic Press.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | IMMUNOGLOBULIN-BINDING DOMAIN; PROTEIN SECONDARY STRUCTURE; NUCLEAR MAGNETIC-RESONANCE; GTPASE-ACTIVATING PROTEIN; COMMON AMINO-ACIDS; NMR-SPECTROSCOPY; SACCHAROMYCES-CEREVISIAE; BIOLOGICAL MACROMOLECULES; RAN/TC4; ENCODES; SUMO-1; ubiquitin; ubiquitin-like proteins; posttranslational modification; nucleocytoplasmic transport |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 02 May 2023 13:37 |
| Last Modified: | 02 May 2023 13:37 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49674 |
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