2uyz
From Proteopedia
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| - | [[Image:2uyz.gif|left|200px]]<br /><applet load="2uyz" size=" | + | [[Image:2uyz.gif|left|200px]]<br /><applet load="2uyz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2uyz, resolution 1.40Å" /> | caption="2uyz, resolution 1.40Å" /> | ||
'''NON-COVALENT COMPLEX BETWEEN UBC9 AND SUMO1'''<br /> | '''NON-COVALENT COMPLEX BETWEEN UBC9 AND SUMO1'''<br /> | ||
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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== | ||
| - | 2UYZ 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 NA 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] Known structural/functional Site: <scene name='pdbsite=AC1:Na Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2UYZ 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=NA:'>NA</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] Known structural/functional Site: <scene name='pdbsite=AC1:Na Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ubl conjugation pathway]] | [[Category: ubl conjugation pathway]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:38:26 2008'' |
Revision as of 12:38, 23 January 2008
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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 with as ligand. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Known structural/functional Site: . 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
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Categories: Homo sapiens | Mus musculus | Protein complex | Ubiquitin--protein ligase | Dijk, W.J.Van. | Knipscheer, P. | Mann, M. | Olsen, J.V. | Sixma, T.K. | NA | Cell cycle | Cell division | Chromosome partition | Conjugating enzyme | E2 | Ligase | Mitosis | Nuclear protein | Sumo1 | Sumoylation | Ubc9 | Ubiquitin-like modifier | Ubl conjugation pathway
