5UDO

Crystal structure of the coiled-coil domain from Listeria Innocua Phage Integrase (Tetragonal Form II)

5UDO の概要

• エントリーDOI: 10.2210/pdb5udo/pdb
• 関連するPDBエントリー: 5U96 5UAE
• 分子名称: A118 serine integrase (2 entities in total)
• 機能のキーワード: site-specific recombination, coiled-coil, recombination
• 由来する生物種: Listeria innocua
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 313245.06

構造登録者

Gupta, K.,Yuan, J.B.,Sharp, R.,Van Duyne, G.D. (登録日: 2016-12-28, 公開日: 2017-06-07, 最終更新日: 2023-10-04)

主引用文献

Gupta, K.,Sharp, R.,Yuan, J.B.,Li, H.,Van Duyne, G.D.
Coiled-coil interactions mediate serine integrase directionality.
Nucleic Acids Res., 45:7339-7353, 2017

PubMed Abstract: Serine integrases are bacteriophage enzymes that carry out site-specific integration and excision of their viral genomes. The integration reaction is highly directional; recombination between the phage attachment site attP and the host attachment site attB to form the hybrid sites attL and attR is essentially irreversible. In a recent model, extended coiled-coil (CC) domains in the integrase subunits are proposed to interact in a way that favors the attPxattB reaction but inhibits the attLxattR reaction. Here, we show for the Listeria innocua integrase (LI Int) system that the CC domain promotes self-interaction in isolated Int and when Int is bound to attachment sites. Three independent crystal structures of the CC domain reveal the molecular nature of the CC dimer interface. Alanine substitutions of key residues in the interface support the functional significance of the structural model and indicate that the same interaction is responsible for promoting integration and for inhibiting excision. An updated model of a LI Int•attL complex that incorporates the high resolution CC dimer structure provides insights that help to explain the unusual CC dimer structure and potential sources of stability in Int•attL and Int•attR complexes. Together, the data provide a molecular basis for understanding serine integrase directionality.

PubMed: 28549184
DOI: 10.1093/nar/gkx474

実験手法

X-RAY DIFFRACTION (2.541 Å)