5gy2

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Crystal structure of a complex between Bacillus subtilis flagellin and zebrafish Toll-like receptor 5Crystal structure of a complex between Bacillus subtilis flagellin and zebrafish Toll-like receptor 5

Structural highlights

5gy2 is a 4 chain structure with sequence from Bacillus subtilis subsp. spizizenii str. W23, Danio rerio and Eptatretus burgeri. 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:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B3DIN1_DANRE Q4G1L2_EPTBU

Publication Abstract from PubMed

Flagellin is a bacterial protein that polymerizes into the flagellar filament and is essential for bacterial motility. When flagellated bacteria invade the host, flagellin is recognized by Toll-like receptor 5 (TLR5) as a pathogen invasion signal and eventually evokes the innate immune response. Here, we provide a conserved structural mechanism by which flagellins from Gram-negative gamma-proteobacteria and Gram-positive Firmicutes bacteria bind and activate TLR5. The comparative structural analysis using our crystal structure of a complex between Bacillus subtilis flagellin (bsflagellin) and TLR5 at 2.1 A resolution, combined with the alanine scanning analysis of the binding interface, reveals a common hot spot in flagellin for TLR5 activation. An arginine residue (bsflagellin R89) of the flagellin D1 domain and its adjacent residues (bsflagellin E114 and L93) constitute a hot spot that provides shape and chemical complementarity to a cavity generated by the loop of leucine-rich repeat 9 in TLR5. In addition to the flagellin D1 domain, the D0 domain also contributes to TLR5 activity through structurally dispersed regions, but not a single focal area. These results establish the groundwork for the future design of flagellin-based therapeutics.

A conserved TLR5 binding and activation hot spot on flagellin.,Song WS, Jeon YJ, Namgung B, Hong M, Yoon SI Sci Rep. 2017 Jan 20;7:40878. doi: 10.1038/srep40878. PMID:28106112[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Song WS, Jeon YJ, Namgung B, Hong M, Yoon SI. A conserved TLR5 binding and activation hot spot on flagellin. Sci Rep. 2017 Jan 20;7:40878. doi: 10.1038/srep40878. PMID:28106112 doi:http://dx.doi.org/10.1038/srep40878

5gy2, resolution 2.10Å

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