2BF8

Crystal structure of SUMO modified ubiquitin conjugating enzyme E2- 25K

2BF8 の概要

• エントリーDOI: 10.2210/pdb2bf8/pdb
• 関連するPDBエントリー: 1A5R 1TGZ 2BEP
• 分子名称: UBIQUITIN-CONJUGATING ENZYME E2-25 KDA, UBIQUITIN-LIKE PROTEIN SMT3C (3 entities in total)
• 機能のキーワード: ligase-complex, e2-25k, e2 ubiquitin conjugating enzyme, sumo, sumo-target structure, ligase, structural proteomics in europe, spine, structural genomics
• 由来する生物種: BOS TAURUS (BOVINE); 詳細
• 細胞内の位置: Cytoplasm: P61085; Nucleus membrane: P63165
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26816.66

構造登録者

Pichler, A.,Knipscheer, P.,Oberhofer, E.,Van Dijk, W.J.,Korner, R.,Velgaard Olsen, J.,Jentsch, S.,Melchior, F.,Sixma, T.K. (登録日: 2004-12-06, 公開日: 2005-02-16, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)