3BTP

Crystal structure of Agrobacterium tumefaciens VirE2 in complex with its chaperone VirE1: a novel fold and implications for DNA binding

3BTP の概要

• エントリーDOI: 10.2210/pdb3btp/pdb
• 分子名称: Single-strand DNA-binding protein, Protein virE1, AMMONIUM ION, ... (5 entities in total)
• 機能のキーワード: tim barrel, unique topology, novel fold, structural genomics, israel structural proteomics center, ispc, crown gall tumor, dna-binding, secreted, virulence, dna binding protein, chaperone
• 由来する生物種: Agrobacterium tumefaciens str.; 詳細
• 細胞内の位置: Secreted: P08062
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70750.90

構造登録者

Dym, O.,Albeck, S.,Unger, T.,Elbaum, M.,Israel Structural Proteomics Center (ISPC) (登録日: 2007-12-30, 公開日: 2008-08-19, 最終更新日: 2024-02-21)

主引用文献

Dym, O.,Albeck, S.,Unger, T.,Jacobovitch, J.,Branzburg, A.,Michael, Y.,Frenkiel-Krispin, D.,Wolf, S.G.,Elbaum, M.
Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners.
Proc.Natl.Acad.Sci.Usa, 105:11170-11175, 2008

PubMed Abstract: Agrobacterium tumefaciens infects its plant hosts by a mechanism of horizontal gene transfer. This capability has led to its widespread use in artificial genetic transformation. In addition to DNA, the bacterium delivers an abundant ssDNA binding protein, VirE2, whose roles in the host include protection from cytoplasmic nucleases and adaptation for nuclear import. In Agrobacterium, VirE2 is bound to its acidic chaperone VirE1. When expressed in vitro in the absence of VirE1, VirE2 is prone to oligomerization and forms disordered filamentous aggregates. These filaments adopt an ordered solenoidal form in the presence of ssDNA, which was characterized previously by electron microscopy and three-dimensional image processing. VirE2 coexpressed in vitro with VirE1 forms a soluble heterodimer. VirE1 thus prevents VirE2 oligomerization and competes with its binding to ssDNA. We present here a crystal structure of VirE2 in complex with VirE1, showing that VirE2 is composed of two independent domains presenting a novel fold, joined by a flexible linker. Electrostatic interactions with VirE1 cement the two domains of VirE2 into a locked form. Comparison with the electron microscopy structure indicates that the VirE2 domains adopt different relative orientations. We suggest that the flexible linker between the domains enables VirE2 to accommodate its different binding partners.

PubMed: 18678909
DOI: 10.1073/pnas.0801525105

実験手法

X-RAY DIFFRACTION (2.3 Å)