4YK3

Crystal Structure of the BID Domain of BepE from Bartonella henselae

Summary for 4YK3

• Entry DOI: 10.2210/pdb4yk3/pdb
• Related: 4YK1 4YK2
• Descriptor: BepE protein, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: ssgcid, bartonella henselae, bepe, virb-translocated bartonella effector protein, bid domain, structural genomics, seattle structural genomics center for infectious disease, protein binding
• Biological source: Bartonella henselae str. Houston-1
• Total number of polymer chains: 4
• Total formula weight: 67001.39

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2015-03-03, release date: 2016-03-09, Last modification date: 2023-09-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)