Structural highlights
Publication Abstract from PubMed
BtpA/Btp1/TcpB is a virulence factor produced by Brucella species that possesses a Toll interleukin-1 receptor (TIR) domain. Once delivered into the host cell, BtpA interacts with MyD88 to interfere with TLR signalling and modulates microtubule dynamics. Here the crystal structure of the BtpA TIR domain at 3.15A is presented. The structure shows a dimeric arrangement of a canonical TIR domain, similar to the Paracoccus denitrificans Tir protein but secured by a unique long N-terminal alpha-tail that packs against the TIR:TIR dimer. Structure-based mutations and multi-angle light scattering experiments characterized the BtpA dimer conformation in solution. The structure of BtpA will help with studies to understand the mechanisms involved in its interactions with MyD88 and with microtubules.
Structure of the Toll/interleukin 1 receptor (TIR) domain of the immunosuppressive Brucella effector BtpA/Btp1/TcpB.,Kaplan-Turkoz B, Koelblen T, Felix C, Candusso MP, O'Callaghan D, Vergunst AC, Terradot L FEBS Lett. 2013 Nov 1;587(21):3412-6. doi: 10.1016/j.febslet.2013.09.007. Epub, 2013 Sep 25. PMID:24076024[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kaplan-Turkoz B, Koelblen T, Felix C, Candusso MP, O'Callaghan D, Vergunst AC, Terradot L. Structure of the Toll/interleukin 1 receptor (TIR) domain of the immunosuppressive Brucella effector BtpA/Btp1/TcpB. FEBS Lett. 2013 Nov 1;587(21):3412-6. doi: 10.1016/j.febslet.2013.09.007. Epub, 2013 Sep 25. PMID:24076024 doi:http://dx.doi.org/10.1016/j.febslet.2013.09.007
