1u4a
From Proteopedia
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| - | [[Image:1u4a.gif|left|200px]] | + | [[Image:1u4a.gif|left|200px]] |
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| - | '''Solution structure of human SUMO-3 C47S''' | + | {{Structure |
| + | |PDB= 1u4a |SIZE=350|CAPTION= <scene name='initialview01'>1u4a</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= SUMO3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of human SUMO-3 C47S''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1U4A is a [ | + | 1U4A 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=1U4A OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of human SUMO-3 C47S and its binding surface for Ubc9., Ding H, Xu Y, Chen Q, Dai H, Tang Y, Wu J, Shi Y, Biochemistry. 2005 Mar 1;44(8):2790-9. PMID:[http:// | + | Solution structure of human SUMO-3 C47S and its binding surface for Ubc9., Ding H, Xu Y, Chen Q, Dai H, Tang Y, Wu J, Shi Y, Biochemistry. 2005 Mar 1;44(8):2790-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15723523 15723523] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: beta beta alpha beta beta alpha beta fold]] | [[Category: beta beta alpha beta beta alpha beta fold]] | ||
| - | ''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 14:27:11 2008'' |
Revision as of 12:27, 20 March 2008
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| Gene: | SUMO3 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of human SUMO-3 C47S
Overview
Small ubiquitin-related modifier SUMO-3 is a member of a growing family of ubiquitin-like proteins (Ubls). So far, four isoforms of SUMO have been identified in humans. It is generally known that SUMO modification regulates protein localization and activity. Previous structure and function studies have been mainly focused on SUMO-1. The sequence of SUMO-3 is 46% identical with that of SUMO-1; nevertheless, functional heterogeneity has been found between the two homologues. Here we report the solution structure of SUMO-3 C47S (residues 14-92) featuring the beta-beta-alpha-beta-beta-alpha-beta ubiquitin fold. Structural comparison shows that SUMO-3 C47S resembles ubiquitin more than SUMO-1. On the helix-sheet interface, a strong hydrophobic interaction contributes to formation of the globular and compact fold. A Gly-Gly motif at the C-terminal tail, extending away from the core structure, is accessible to enzymes and substrates. In vivo, SUMO modification proceeds via a multistep pathway, and Ubc9 plays an indispensable role as the SUMO conjugating enzyme (E2) in this process. To develop a better understanding of SUMO-3 conjugation, the Ubc9 binding surface on SUMO-3 C47S has been detected by chemical shift perturbation using NMR spectroscopy. The binding site mainly resides on the hydrophilic side of the beta-sheet. Negatively charged and hydrophobic residues of this region are highly or moderately conserved among SUMO family members. Notably, the negatively charged surface of SUMO-3 C47S is highly complementary in its electrostatic potentials and hydrophobicity to the positively charged surface of Ubc9. This work indicates dissimilarities between SUMO-3 and SUMO-1 in tertiary structure and provides insight into the specific interactions of SUMO-3 with its modifying enzyme.
About this Structure
1U4A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human SUMO-3 C47S and its binding surface for Ubc9., Ding H, Xu Y, Chen Q, Dai H, Tang Y, Wu J, Shi Y, Biochemistry. 2005 Mar 1;44(8):2790-9. PMID:15723523
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