4yk1 | pdb_00004yk1

Crystal Structure of the BID Domain of Bep6 from Bartonella rochalimae

spinqualitylabelsall models 4yk1, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yk1 is a 1 chain structure with sequence from Bartonella rochalimae ATCC BAA-1498. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E6YLF3_9HYPH Publication Abstract from PubMed 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. The BID Domain of Type IV Secretion Substrates Forms a Conserved Four-Helix Bundle Topped with a Hook.,Stanger FV, de Beer TA, Dranow DM, Schirmer T, Phan I, Dehio C Structure. 2017 Jan 3;25(1):203-211. doi: 10.1016/j.str.2016.10.010. Epub 2016, Nov 23. PMID:27889208 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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