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1a5r
From Proteopedia
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| - | [[Image:1a5r.gif|left|200px]] | + | [[Image:1a5r.gif|left|200px]] |
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| - | '''STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED MODIFIER SUMO-1, NMR, 10 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1a5r |SIZE=350|CAPTION= <scene name='initialview01'>1a5r</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED MODIFIER SUMO-1, NMR, 10 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A5R is a [ | + | 1A5R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A5R OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9654451 9654451] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sumo-1]] | [[Category: sumo-1]] | ||
[[Category: targeting protein]] | [[Category: targeting protein]] | ||
| - | [[Category: ubiquitin-like | + | [[Category: ubiquitin-like protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:17 2008'' |
Revision as of 07:53, 20 March 2008
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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 Thu Mar 20 09:53:17 2008
