A steric antagonism of actin polymerization by a Salmonella virulence protein
A steric antagonism of actin polymerization by a Salmonella virulence protein
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DOI：
10.1016/j.str.2006.05.022
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发表时间：
2006-08-01
期刊：
影响因子：
5.7
通讯作者：
Stebbins, C. Erec
中科院分区：
文献类型：
--
作者：
Margarit, S. Mariana;Davidson, Walter;Stebbins, C. Erec
Salmonella spp. require the ADP-ribosyltransferase activity of the SpvB protein for intracellular growth and systemic virulence. SpvB covalently modifies actin, causing cytoskeletal disruption and apoptosis. We report here the crystal structure of the catalytic domain of SpvB, and we show by mass spectrometric analysis that SpvB modifies actin at Arg177, inhibiting its ATPase activity. We also describe two crystal structures of SpvB-modified, polymerization-deficient actin. These structures reveal that ADP-ribosylation does not lead to dramatic conformational changes in actin, suggesting a model in which this large family of toxins inhibits actin polymerization primarily through steric disruption of intrafilament contacts.
