2bf8: Difference between revisions

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New page: left|200px<br /> <applet load="2bf8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bf8, resolution 2.30Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:2bf8.gif|left|200px]]<br />
[[Image:2bf8.gif|left|200px]]<br /><applet load="2bf8" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2bf8" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2bf8, resolution 2.30&Aring;" />
caption="2bf8, resolution 2.30&Aring;" />
'''CRYSTAL STRUCTURE OF SUMO MODIFIED UBIQUITIN CONJUGATING ENZYME E2-25K'''<br />
'''CRYSTAL STRUCTURE OF SUMO MODIFIED UBIQUITIN CONJUGATING ENZYME E2-25K'''<br />


==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 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.
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.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
2BF8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA].  
2BF8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=2BF8 OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Dijk, W.J.Van.]]
[[Category: Dijk, W J.Van.]]
[[Category: Jentsch, S.]]
[[Category: Jentsch, S.]]
[[Category: Knipscheer, P.]]
[[Category: Knipscheer, P.]]
Line 25: Line 24:
[[Category: Melchior, F.]]
[[Category: Melchior, F.]]
[[Category: Oberhofer, E.]]
[[Category: Oberhofer, E.]]
[[Category: Olsen, J.Velgaard.]]
[[Category: Olsen, J Velgaard.]]
[[Category: Pichler, A.]]
[[Category: Pichler, A.]]
[[Category: SPINE, Structural.Proteomics.in.Europe.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: Sixma, T.K.]]
[[Category: Sixma, T K.]]
[[Category: e2 ubiquitin conjugating enzyme]]
[[Category: e2 ubiquitin conjugating enzyme]]
[[Category: e2-25k]]
[[Category: e2-25k]]
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[[Category: sumo-target structure]]
[[Category: sumo-target structure]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:02:03 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:12 2008''

Revision as of 17:37, 21 February 2008

File:2bf8.gif


2bf8, resolution 2.30Å

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CRYSTAL STRUCTURE OF SUMO MODIFIED UBIQUITIN CONJUGATING ENZYME E2-25K

OverviewOverview

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.

DiseaseDisease

Known diseases associated with this structure: Orofacial cleft 10 OMIM:[601912]

About this StructureAbout this Structure

2BF8 is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.

ReferenceReference

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

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