Structural highlights
Function
BP26_BRUA1
Publication Abstract from PubMed
An outer membrane protein BP26/OMP28 of Brucella, BP26, is identified as a major immunodominant antigen and widely used as a diagnostic marker and for vaccination against Brucellosis. BP26 belongs to the family of proteins that contains a SIMPL (signaling molecule that associates with the mouse pelle-like kinase) domain, whose structure and function have been unknown. Here, we present the crystal structure of BP26 revealing that 16 BP26 molecules form a novel channel-like assembly as also shown by electron microscopy analysis. Eight BP26 molecules forming a ring structure contain a hole at the center of the octamer, and another octamer interacts with each other to form a channel having a large internal cavity. BP26 is found to be structurally similar to a bacteriophage protein involved in infection, implicating that BP26 might function during Brucella infection. In addition, the BP26 structure suggests that the protein functions as a multimeric channel-like form and provides a canonical model for the SIMPL domains.
Brucella Immunogenic BP26 Forms a Channel-like Structure.,Kim D, Park J, Kim SJ, Soh YM, Kim HM, Oh BH, Song JJ J Mol Biol. 2013 Jan 23. pii: S0022-2836(13)00031-4. doi:, 10.1016/j.jmb.2013.01.015. PMID:23353825[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim D, Park J, Kim SJ, Soh YM, Kim HM, Oh BH, Song JJ. Brucella Immunogenic BP26 Forms a Channel-like Structure. J Mol Biol. 2013 Jan 23. pii: S0022-2836(13)00031-4. doi:, 10.1016/j.jmb.2013.01.015. PMID:23353825 doi:http://dx.doi.org/10.1016/j.jmb.2013.01.015