2bep
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Post-translational modification with small ubiquitin-related modifier, (SUMO) alters the function of many proteins, but the molecular mechanisms, and consequences of this modification are still poorly defined. During a, screen for novel SUMO1 targets, we identified the ubiquitin-conjugating, enzyme E2-25K (Hip2). SUMO attachment severely impairs E2-25K ubiquitin, thioester and unanchored ubiquitin chain formation in vitro. Crystal, structures of E2-25K(1-155) and of the E2-25K(1-155)-SUMO conjugate, (E2-25K(*)SUMO) indicate that SUMO attachment interferes with E1, interaction through its location on the N-terminal helix. The SUMO, acceptor site in E2-25K, Lys14, does not conform to the consensus site, found in most SUMO targets (PsiKXE), and functions only in the context of, an ... | + | Post-translational modification with small ubiquitin-related modifier, (SUMO) alters the function of many proteins, but the molecular mechanisms, and consequences of this modification are still poorly defined. During a, screen for novel SUMO1 targets, we identified the ubiquitin-conjugating, enzyme E2-25K (Hip2). SUMO attachment severely impairs E2-25K ubiquitin, thioester and unanchored ubiquitin chain formation in vitro. Crystal, structures of E2-25K(1-155) and of the E2-25K(1-155)-SUMO conjugate, (E2-25K(*)SUMO) indicate that SUMO attachment interferes with E1, interaction through its location on the N-terminal helix. The SUMO, acceptor site in E2-25K, Lys14, does not conform to the consensus site, found in most SUMO targets (PsiKXE), and functions only in the context of, an alpha-helix. In contrast, adjacent SUMO consensus sites are modified, only when in unstructured peptides. The demonstration that secondary, structure elements are part of SUMO attachment signals could contribute to, a better prediction of SUMO targets. |
==About this Structure== | ==About this Structure== | ||
| - | 2BEP is a | + | 2BEP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with BME 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BEP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:54:34 2007'' |
Revision as of 12:49, 5 November 2007
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CRYSTAL STRUCTURE OF UBIQUITIN CONJUGATING ENZYME E2-25K
Overview
Post-translational modification with small ubiquitin-related modifier, (SUMO) alters the function of many proteins, but the molecular mechanisms, and consequences of this modification are still poorly defined. During a, screen for novel SUMO1 targets, we identified the ubiquitin-conjugating, enzyme E2-25K (Hip2). SUMO attachment severely impairs E2-25K ubiquitin, thioester and unanchored ubiquitin chain formation in vitro. Crystal, structures of E2-25K(1-155) and of the E2-25K(1-155)-SUMO conjugate, (E2-25K(*)SUMO) indicate that SUMO attachment interferes with E1, interaction through its location on the N-terminal helix. The SUMO, acceptor site in E2-25K, Lys14, does not conform to the consensus site, found in most SUMO targets (PsiKXE), and functions only in the context of, an alpha-helix. In contrast, adjacent SUMO consensus sites are modified, only when in unstructured peptides. The demonstration that secondary, structure elements are part of SUMO attachment signals could contribute to, a better prediction of SUMO targets.
About this Structure
2BEP is a Single protein structure of sequence from Bos taurus with BME as ligand. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
SUMO modification of the ubiquitin-conjugating enzyme E2-25K., Pichler A, Knipscheer P, Oberhofer E, van Dijk WJ, Korner R, Olsen JV, Jentsch S, Melchior F, Sixma TK, Nat Struct Mol Biol. 2005 Mar;12(3):264-9. Epub 2005 Feb 20. PMID:15723079
Page seeded by OCA on Mon Nov 5 14:54:34 2007
Categories: Bos taurus | Single protein | Ubiquitin--protein ligase | Dijk, W.J.Van. | Jentsch, S. | Knipscheer, P. | Korner, R. | Melchior, F. | Oberhofer, E. | Olsen, J.Velgaard. | Pichler, A. | SPINE, Structural.Proteomics.in.Europe. | Sixma, T.K. | BME | E2 conjugating enzyme | Ligase | Protein degradation | Spine | Structural genomics | Structural proteomics in europe | Ubiquitin
