Structure of the InIB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L-monocytogenes
Structure of the InIB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L-monocytogenes
复制标题
DOI：
10.1016/s1097-2765(00)80234-8
复制
发表时间：
1999-12-01
期刊：
影响因子：
16
通讯作者：
Ghosh, P
中科院分区：
文献类型：
--
作者：
Marino, M;Braun, L;Ghosh, P
The L. monocytogenes protein InIB activates phosphoinositide 3-kinase and induces phagocytosis in several mammalian cell types. The 1.86 Angstrom resolution X-ray crystal structure of the leucine-rich repeat domain of InIB that is both necessary and sufficient to induce phagocytosis is presented here. The structure supports a crucial role for calcium in host cell invasion by L. monocytogenes and supplies a rationale for its function. Calciums are bound to the protein in an unusually exposed manner that suggests that the metals may act as a bridge between InIB and mammalian cell surface receptors. The structure also identifies surfaces on the curved and elongated molecule that may constitute additional interaction sites in forming a bacterial-mammalian signaling complex.
