4J2N

Crystal Structure of mycobacteriophage Pukovnik Xis

4J2N の概要

• エントリーDOI: 10.2210/pdb4j2n/pdb
• 分子名称: Gp37, SULFATE ION (3 entities in total)
• 機能のキーワード: winged-helix, doman swap, filament, viral protein
• 由来する生物種: Mycobacterium phage Pukovnik
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 32801.59

構造登録者

Homa, N.J.,Amrich, C.G.,Heroux, A.,VanDemark, A.P. (登録日: 2013-02-04, 公開日: 2013-10-23, 最終更新日: 2024-02-28)

主引用文献

Singh, S.,Plaks, J.G.,Homa, N.J.,Amrich, C.G.,Heroux, A.,Hatfull, G.F.,Vandemark, A.P.
The Structure of Xis Reveals the Basis for Filament Formation and Insight into DNA Bending within a Mycobacteriophage Intasome.
J.Mol.Biol., 426:412-422, 2014

PubMed Abstract: The recombination directionality factor, Xis, is a DNA bending protein that determines the outcome of integrase-mediated site-specific recombination by redesign of higher-order protein-DNA architectures. Although the attachment site DNA of mycobacteriophage Pukovnik is likely to contain four sites for Xis binding, Xis crystals contain five subunits in the asymmetric unit, four of which align into a Xis filament and a fifth that is generated by an unusual domain swap. Extensive intersubunit contacts stabilize a bent filament-like arrangement with Xis monomers aligned head to tail. The structure implies a DNA bend of ~120°, which is in agreement with DNA bending measured in vitro. Formation of attR-containing intasomes requires only Int and Xis, distinguishing Pukovnik from lambda. Therefore, we conclude that, in Pukovnik, Xis-induced DNA bending is sufficient to promote intramolecular Int-mediated bridges during intasome formation.

PubMed: 24112940
DOI: 10.1016/j.jmb.2013.10.002

実験手法

X-RAY DIFFRACTION (2.348 Å)