组蛋白八聚体
富含亮氨酸重复
生物
布鲁氏菌
计算生物学
细胞生物学
结晶学
化学
遗传学
DNA
激酶
病毒学
组蛋白
核小体
布鲁氏菌病
作者
Daegeun Kim,Jihye Park,Soo Jin Kim,Young‐Min Soh,Ho Min Kim,Byung‐Ha Oh,Ji‐Joon Song
标识
DOI:10.1016/j.jmb.2013.01.015
摘要
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.
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