1a5r
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a5r OCA], [http://www.ebi.ac.uk/pdbsum/1a5r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a5r RCSB]</span> | ||
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[[Category: ubiquitin-like protein]] | [[Category: ubiquitin-like protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:33:49 2008'' |
Revision as of 15:33, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED MODIFIER SUMO-1, NMR, 10 STRUCTURES
Overview
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 betabetaalphabetabetaalphabeta 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.
About this Structure
1A5R is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure determination of the small ubiquitin-related modifier SUMO-1., Bayer P, Arndt A, Metzger S, Mahajan R, Melchior F, Jaenicke R, Becker J, J Mol Biol. 1998 Jul 10;280(2):275-86. PMID:9654451
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