4YK1

Crystal Structure of the BID Domain of Bep6 from Bartonella rochalimae

4YK1 の概要

• エントリーDOI: 10.2210/pdb4yk1/pdb
• 関連するPDBエントリー: 4YK2 4YK3
• 分子名称: Bartonella effector protein (Bep) substrate of VirB T4SS (2 entities in total)
• 機能のキーワード: ssgcid, bartonella rochalimae, bep6, virb-translocated bartonella effector protein, bid domain, structural genomics, seattle structural genomics center for infectious disease, protein binding
• 由来する生物種: Bartonella rochalimae ATCC BAA-1498
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17192.29

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2015-03-03, 公開日: 2016-03-09, 最終更新日: 2024-10-23)

主引用文献

Stanger, F.V.,de Beer, T.A.,Dranow, D.M.,Schirmer, T.,Phan, I.,Dehio, C.
The BID Domain of Type IV Secretion Substrates Forms a Conserved Four-Helix Bundle Topped with a Hook.
Structure, 25:203-211, 2017

PubMed Abstract: The BID (Bep intracellular delivery) domain functions as secretion signal in a subfamily of protein substrates of bacterial type IV secretion (T4S) systems. It mediates transfer of (1) relaxases and the attached DNA during bacterial conjugation, and (2) numerous Bartonella effector proteins (Beps) during protein transfer into host cells infected by pathogenic Bartonella species. Furthermore, BID domains of Beps have often evolved secondary effector functions within host cells. Here, we provide crystal structures for three representative BID domains and describe a novel conserved fold characterized by a compact, antiparallel four-helix bundle topped with a hook. The conserved hydrophobic core provides a rigid scaffold to a surface that, despite a few conserved exposed residues and similarities in charge distribution, displays significant variability. We propose that the genuine function of BID domains as T4S signal may primarily depend on their rigid structure, while the plasticity of their surface may facilitate adaptation to secondary effector functions.

PubMed: 27889208
DOI: 10.1016/j.str.2016.10.010

実験手法

X-RAY DIFFRACTION (2.1 Å)