Crystal structure of the passenger domain of the Escherichia coli autotransporter EspP.
Crystal structure of the passenger domain of the Escherichia coli autotransporter EspP.
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DOI:
10.1016/j.jmb.2011.09.028
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发表时间:
2011-11-11
影响因子:
5.6
通讯作者:
Pai, Emil F.
中科院分区:
文献类型:
--
作者:
Khan, Shekeb;Mian, Hira S.;Sandercock, Linda E.;Chirgadze, Nickolay Y.;Pai, Emil F.
Autotransporters represent a large superfamily of known and putative virulence factors produced by Gram-negative bacteria. They consist of an N-terminal “passenger domain” responsible for the specific effector functions of the molecule and a C-terminal “β domain” responsible for translocation of the passenger across the bacterial outer membrane. Here we present the 2.5-Å crystal structure of the passenger domain of the extracellular serine protease EspP, produced by the pathogen Escherichia coli O157:H7 and a member of the serine protease autotransporters of Enterobacteriaceae (SPATEs). Like the previously structurally characterized SPATE passenger domains, the EspP passenger domain contains an extended right-handed parallel β-helix preceded by an N-terminal globular domain housing the catalytic function of the protease. Of note, however, is the absence of a second globular domain protruding from this β- helix. We describe the structure of the EspP passenger domain in the context of previous results and provide an alternative hypothesis for the function of the β-helix within SPATEs.
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