3RD2

NIP45 SUMO-like Domain 2

3RD2 の概要

• エントリーDOI: 10.2210/pdb3rd2/pdb
• 分子名称: NFATC2-interacting protein (2 entities in total)
• 機能のキーワード: sumo-like domain 2, protein:protein interaction, ubc9, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus (By similarity): Q8NCF5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9366.60

構造登録者

Perry, J.J.P.,Arvai, A.S.,Tainer, J.A. (登録日: 2011-03-31, 公開日: 2011-04-27, 最終更新日: 2023-09-13)

主引用文献

Prudden, J.,Perry, J.J.,Nie, M.,Vashisht, A.A.,Arvai, A.S.,Hitomi, C.,Guenther, G.,Wohlschlegel, J.A.,Tainer, J.A.,Boddy, M.N.
DNA repair and global sumoylation are regulated by distinct Ubc9 noncovalent complexes.
Mol.Cell.Biol., 31:2299-2310, 2011

PubMed Abstract: Global sumoylation, SUMO chain formation, and genome stabilization are all outputs generated by a limited repertoire of enzymes. Mechanisms driving selectivity for each of these processes are largely uncharacterized. Here, through crystallographic analyses we show that the SUMO E2 Ubc9 forms a noncovalent complex with a SUMO-like domain of Rad60 (SLD2). Ubc9:SLD2 and Ubc9:SUMO noncovalent complexes are structurally analogous, suggesting that differential recruitment of Ubc9 by SUMO or Rad60 provides a novel means for such selectivity. Indeed, deconvoluting Ubc9 function by disrupting either the Ubc9:SLD2 or Ubc9:SUMO noncovalent complex reveals distinct roles in facilitating sumoylation. Ubc9:SLD2 acts in the Nse2 SUMO E3 ligase-dependent pathway for DNA repair, whereas Ubc9:SUMO instead promotes global sumoylation and chain formation, via the Pli1 E3 SUMO ligase. Moreover, this Pli1-dependent SUMO chain formation causes the genome instability phenotypes of SUMO-targeted ubiquitin ligase (STUbL) mutants. Overall, we determine that, unexpectedly, Ubc9 noncovalent partner choice dictates the role of sumoylation in distinct cellular pathways.

PubMed: 21444718
DOI: 10.1128/MCB.05188-11

実験手法

X-RAY DIFFRACTION (1.6 Å)