کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2184821 | 1095935 | 2013 | 8 صفحه PDF | دانلود رایگان |
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.
Graphical AbstractFigure optionsDownload high-quality image (415 K)Download as PowerPoint slideHighlights
► Crystal structure of an immunogenic protein BP26 from Brucella abortus.
► BP26 forms a homo-hexadecamer with an internal channel.
► The structure of BP26 represents the first structure of the SIMPL domains.
Journal: Journal of Molecular Biology - Volume 425, Issue 7, 12 April 2013, Pages 1119–1126