2BEP

Crystal structure of ubiquitin conjugating enzyme E2-25K

Summary for 2BEP

• Entry DOI: 10.2210/pdb2bep/pdb
• Related: 2BF8
• Descriptor: UBIQUITIN-CONJUGATING ENZYME E2-25 KDA, BETA-MERCAPTOETHANOL (3 entities in total)
• Functional Keywords: ligase, ubiquitin, e2 conjugating enzyme, protein degradation, structural proteomics in europe, spine, structural genomics
• Biological source: BOS TAURUS (BOVINE)
• Cellular location: Cytoplasm: P61085
• Total number of polymer chains: 1
• Total formula weight: 17924.55

Authors

Pichler, A.,Knipscheer, P.,Oberhofer, E.,Van Dijk, W.J.,Korner, R.,Velgaard Olsen, J.,Jentsch, S.,Melchior, F.,Sixma, T.K. (deposition date: 2004-11-29, release date: 2005-02-16, Last modification date: 2023-12-13)

Primary citation

Pichler, A.,Knipscheer, P.,Oberhofer, E.,Van Dijk, W.J.,Korner, R.,Velgaard Olsen, J.,Jentsch, S.,Melchior, F.,Sixma, T.K.
Sumo Imodification of the Ubiquitin Conjugating Enzyme E2-25K
Nat.Struct.Mol.Biol., 12:264-, 2005

PubMed Abstract: 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.

PubMed: 15723079
DOI: 10.1038/NSMB903

Experimental method

X-RAY DIFFRACTION (1.8 Å)