2bep: Difference between revisions

Line 4:

==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.

==About this Structure==

Line 14:

[[Category: Single protein]]

[[Category: Ubiquitin--protein ligase]]

[[Category: Dijk, W.J.Van.]]

[[Category: Dijk, W J.Van.]]

[[Category: Jentsch, S.]]

[[Category: Knipscheer, P.]]

Line 20:

[[Category: Melchior, F.]]

[[Category: Oberhofer, E.]]

[[Category: Olsen, J.Velgaard.]]

[[Category: Olsen, J Velgaard.]]

[[Category: Pichler, A.]]

[[Category: SPINE, Structural.Proteomics.in.Europe.]]

[[Category: SPINE, Structural Proteomics in Europe.]]

[[Category: Sixma, T.K.]]

[[Category: Sixma, T K.]]

[[Category: BME]]

[[Category: e2 conjugating enzyme]]

Line 33:

[[Category: ubiquitin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 10~~:23:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:02 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Ubiquitin--protein ligase]]
-[[Category: Dijk, W.J.Van.]]
+[[Category: Dijk, W J.Van.]]
 [[Category: Jentsch, S.]]
 [[Category: Knipscheer, P.]]
@@ Line 20: / Line 20: @@
 [[Category: Melchior, F.]]
 [[Category: Oberhofer, E.]]
-[[Category: Olsen, J.Velgaard.]]
+[[Category: Olsen, J Velgaard.]]
 [[Category: Pichler, A.]]
-[[Category: SPINE, Structural.Proteomics.in.Europe.]]
+[[Category: SPINE, Structural Proteomics in Europe.]]
-[[Category: Sixma, T.K.]]
+[[Category: Sixma, T K.]]
 [[Category: BME]]
 [[Category: e2 conjugating enzyme]]
@@ Line 33: / Line 33: @@
 [[Category: ubiquitin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:23:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:02 2008''