This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1a5r
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1a5r.gif|left|200px]] | [[Image:1a5r.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1a5r", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1a5r| PDB=1a5r | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED MODIFIER SUMO-1, NMR, 10 STRUCTURES''' | '''STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED MODIFIER SUMO-1, NMR, 10 STRUCTURES''' | ||
| Line 32: | Line 29: | ||
[[Category: Melchior, F.]] | [[Category: Melchior, F.]] | ||
[[Category: Metzger, S.]] | [[Category: Metzger, S.]] | ||
| - | [[Category: | + | [[Category: Post-translational protein modification]] |
| - | [[Category: | + | [[Category: Sumo-1]] |
| - | [[Category: | + | [[Category: Targeting protein]] |
| - | [[Category: | + | [[Category: Ubiquitin-like protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:51:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:51, 2 May 2008
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 Page seeded by OCA on Fri May 2 09:51:07 2008
