4BVU

Structure of Shigella effector OspG in complex with host UbcH5c- Ubiquitin conjugate

4BVU の概要

• エントリーDOI: 10.2210/pdb4bvu/pdb
• 分子名称: PROTEIN KINASE OSPG, UBIQUITIN-CONJUGATING ENZYME E2 D3, UBIQUITIN, ... (4 entities in total)
• 機能のキーワード: transferase-ligase-protein binding complex, kinase, transferase/ligase/protein binding
• 由来する生物種: SHIGELLA FLEXNERI; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 49657.24

構造登録者

Pruneda, J.N.,LeTrong, I.,Stenkamp, R.E.,Klevit, R.E.,Brzovic, P.S. (登録日: 2013-06-28, 公開日: 2014-01-29, 最終更新日: 2023-12-20)

主引用文献

Pruneda, J.N.,Smith, F.D.,Daurie, A.,Swaney, D.L.,Villen, J.,Scott, J.D.,Stadnyk, A.W.,Le Trong, I.,Stenkamp, R.E.,Klevit, R.E.,Rohde, J.R.,Brzovic, P.S.
E2~Ub Conjugates Regulate the Kinase Activity of Shigella Effector Ospg During Pathogenesis.
Embo J., 33:437-, 2014

PubMed Abstract: Pathogenic bacteria introduce effector proteins directly into the cytosol of eukaryotic cells to promote invasion and colonization. OspG, a Shigella spp. effector kinase, plays a role in this process by helping to suppress the host inflammatory response. OspG has been reported to bind host E2 ubiquitin-conjugating enzymes activated with ubiquitin (E2~Ub), a key enzyme complex in ubiquitin transfer pathways. A co-crystal structure of the OspG/UbcH5c~Ub complex reveals that complex formation has important ramifications for the activity of both OspG and the UbcH5c~Ub conjugate. OspG is a minimal kinase domain containing only essential elements required for catalysis. UbcH5c~Ub binding stabilizes an active conformation of the kinase, greatly enhancing OspG kinase activity. In contrast, interaction with OspG stabilizes an extended, less reactive form of UbcH5c~Ub. Recognizing conserved E2 features, OspG can interact with at least ten distinct human E2s~Ub. Mouse oral infection studies indicate that E2~Ub conjugates act as novel regulators of OspG effector kinase function in eukaryotic host cells.

PubMed: 24446487
DOI: 10.1002/EMBJ.201386386

実験手法

X-RAY DIFFRACTION (2.7 Å)