细菌应激传感器的变构激活

Allosteric activation of a bacterial stress sensor.

作者信息

Yan Nieng, Shi Yigong

机构信息

Center for Structural Biology, Institute of Biomedicine, Tsinghua University, Beijing, China.

出版信息

Cell. 2007 Nov 2;131(3):441-3. doi: 10.1016/j.cell.2007.10.021.

DOI:10.1016/j.cell.2007.10.021

PMID:17981109

Abstract

In Gram-negative bacteria, envelope stress signals such as unfolded outer membrane proteins (OMP) activate the periplasmic protease DegS. This protease then triggers a cellular pathway to alleviate the stress. Now Sohn et al. (2007) show conclusively that inhibition of DegS is relieved allosterically by binding of the C-terminal sequences in unfolded OMPs to the PDZ domain of DegS.

摘要

在革兰氏阴性菌中，诸如未折叠的外膜蛋白（OMP）等包膜应激信号会激活周质蛋白酶DegS。然后这种蛋白酶会触发一条细胞途径来缓解应激。现在， Sohn等人（2007年）确凿地表明，未折叠的OMP中的C末端序列与DegS的PDZ结构域结合，会通过变构作用解除对DegS的抑制。