1kps
From Proteopedia
(New page: 200px<br /> <applet load="1kps" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kps, resolution 2.50Å" /> '''Structural Basis fo...) |
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| - | [[Image:1kps.gif|left|200px]]<br /> | + | [[Image:1kps.gif|left|200px]]<br /><applet load="1kps" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1kps" size=" | + | |
caption="1kps, resolution 2.50Å" /> | caption="1kps, resolution 2.50Å" /> | ||
'''Structural Basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin conjugating enzyme Ubc9 and RanGAP1'''<br /> | '''Structural Basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin conjugating enzyme Ubc9 and RanGAP1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | E2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to | + | E2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues directly or through E3-mediated reactions. The small ubiquitin-like modifier SUMO regulates nuclear transport, stress response, and signal transduction in eukaryotes and is essential for cell-cycle progression in yeast. In contrast to most ubiquitin conjugation, the SUMO E2 enzyme Ubc9 is sufficient for substrate recognition and lysine modification of known SUMO targets. Crystallographic analysis of a complex between mammalian Ubc9 and a C-terminal domain of RanGAP1 at 2.5 A reveals structural determinants for recognition of consensus SUMO modification sequences found within SUMO-conjugated proteins. Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1. |
==About this Structure== | ==About this Structure== | ||
| - | 1KPS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http:// | + | 1KPS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KPS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ubiquitin--protein ligase]] | [[Category: Ubiquitin--protein ligase]] | ||
[[Category: Bernier-Villamor, V.]] | [[Category: Bernier-Villamor, V.]] | ||
| - | [[Category: Lima, C | + | [[Category: Lima, C D.]] |
| - | [[Category: Matunis, M | + | [[Category: Matunis, M J.]] |
| - | [[Category: Sampson, D | + | [[Category: Sampson, D A.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: conjugating enzyme]] | [[Category: conjugating enzyme]] | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:37 2008'' |
Revision as of 11:36, 21 February 2008
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Structural Basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin conjugating enzyme Ubc9 and RanGAP1
Overview
E2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues directly or through E3-mediated reactions. The small ubiquitin-like modifier SUMO regulates nuclear transport, stress response, and signal transduction in eukaryotes and is essential for cell-cycle progression in yeast. In contrast to most ubiquitin conjugation, the SUMO E2 enzyme Ubc9 is sufficient for substrate recognition and lysine modification of known SUMO targets. Crystallographic analysis of a complex between mammalian Ubc9 and a C-terminal domain of RanGAP1 at 2.5 A reveals structural determinants for recognition of consensus SUMO modification sequences found within SUMO-conjugated proteins. Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1.
About this Structure
1KPS is a Protein complex structure of sequences from Homo sapiens and Mus musculus with as ligand. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.
Reference
Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1., Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD, Cell. 2002 Feb 8;108(3):345-56. PMID:11853669
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