2uyz
From Proteopedia
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|PDB= 2uyz |SIZE=350|CAPTION= <scene name='initialview01'>2uyz</scene>, resolution 1.40Å | |PDB= 2uyz |SIZE=350|CAPTION= <scene name='initialview01'>2uyz</scene>, resolution 1.40Å | ||
|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyz OCA], [http://www.ebi.ac.uk/pdbsum/2uyz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2uyz RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The ubiquitin-related modifier SUMO regulates a wide range of cellular processes by post-translational modification with one, or a chain of SUMO molecules. Sumoylation is achieved by the sequential action of several enzymes in which the E2, Ubc9, transfers SUMO from the E1 to the target mostly with the help of an E3 enzyme. In this process, Ubc9 not only forms a thioester bond with SUMO, but also interacts with SUMO noncovalently. Here, we show that this noncovalent interaction promotes the formation of short SUMO chains on targets such as Sp100 and HDAC4. We present a crystal structure of the noncovalent Ubc9-SUMO1 complex, showing that SUMO is located far from the E2 active site and resembles the noncovalent interaction site for ubiquitin on UbcH5c and Mms2. Structural comparison suggests a model for poly-sumoylation involving a mechanism analogous to Mms2-Ubc13-mediated ubiquitin chain formation. | The ubiquitin-related modifier SUMO regulates a wide range of cellular processes by post-translational modification with one, or a chain of SUMO molecules. Sumoylation is achieved by the sequential action of several enzymes in which the E2, Ubc9, transfers SUMO from the E1 to the target mostly with the help of an E3 enzyme. In this process, Ubc9 not only forms a thioester bond with SUMO, but also interacts with SUMO noncovalently. Here, we show that this noncovalent interaction promotes the formation of short SUMO chains on targets such as Sp100 and HDAC4. We present a crystal structure of the noncovalent Ubc9-SUMO1 complex, showing that SUMO is located far from the E2 active site and resembles the noncovalent interaction site for ubiquitin on UbcH5c and Mms2. Structural comparison suggests a model for poly-sumoylation involving a mechanism analogous to Mms2-Ubc13-mediated ubiquitin chain formation. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Orofacial cleft 10 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601912 601912]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Olsen, J V.]] | [[Category: Olsen, J V.]] | ||
[[Category: Sixma, T K.]] | [[Category: Sixma, T K.]] | ||
| - | [[Category: NA]] | ||
[[Category: cell cycle]] | [[Category: cell cycle]] | ||
[[Category: cell division]] | [[Category: cell division]] | ||
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[[Category: ubl conjugation pathway]] | [[Category: ubl conjugation pathway]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:06:26 2008'' |
Revision as of 02:06, 31 March 2008
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| , resolution 1.40Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Ubiquitin--protein ligase, with EC number 6.3.2.19 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NON-COVALENT COMPLEX BETWEEN UBC9 AND SUMO1
Overview
The ubiquitin-related modifier SUMO regulates a wide range of cellular processes by post-translational modification with one, or a chain of SUMO molecules. Sumoylation is achieved by the sequential action of several enzymes in which the E2, Ubc9, transfers SUMO from the E1 to the target mostly with the help of an E3 enzyme. In this process, Ubc9 not only forms a thioester bond with SUMO, but also interacts with SUMO noncovalently. Here, we show that this noncovalent interaction promotes the formation of short SUMO chains on targets such as Sp100 and HDAC4. We present a crystal structure of the noncovalent Ubc9-SUMO1 complex, showing that SUMO is located far from the E2 active site and resembles the noncovalent interaction site for ubiquitin on UbcH5c and Mms2. Structural comparison suggests a model for poly-sumoylation involving a mechanism analogous to Mms2-Ubc13-mediated ubiquitin chain formation.
About this Structure
2UYZ is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation., Knipscheer P, van Dijk WJ, Olsen JV, Mann M, Sixma TK, EMBO J. 2007 Jun 6;26(11):2797-807. Epub 2007 May 10. PMID:17491593
Page seeded by OCA on Mon Mar 31 05:06:26 2008
Categories: Homo sapiens | Mus musculus | Protein complex | Ubiquitin--protein ligase | Dijk, W J.Van. | Knipscheer, P. | Mann, M. | Olsen, J V. | Sixma, T K. | Cell cycle | Cell division | Chromosome partition | Conjugating enzyme | E2 | Ligase | Mitosis | Nuclear protein | Sumo1 | Sumoylation | Ubc9 | Ubiquitin-like modifier | Ubl conjugation pathway
