PMC:2724173 / 4222-5219 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/2724173","sourcedb":"PMC","sourceid":"2724173","source_url":"https://www.ncbi.nlm.nih.gov/pmc/2724173","text":"There are, however, several differences between the members of this family. Most notably, activation of type 3 secretion in Yersinia sp. results in the secretion of YopN, while TyeA remains in the bacterial cytoplasm.15,16 The dissociation of YopN and TyeA has been proposed as a mechanism for the regulation of secretion but clearly cannot be a conserved mechanism in those species where the homologue is a single polypeptide chain.17 In the crystal structure of the Y. pestis YopN-TyeA complex, the close proximity of the C terminus of YopN with the N terminus of TyeA suggested that a single polypeptide encoding both proteins could maintain the same overall structure.5 In order to confirm this, we have determined and refined the structure of the S. flexneri homologue, MxiC, in three distinct crystal forms. The molecular architecture and movement of the domains of MxiC compared with that of YopN-TyeA highlights conformational differences that may play an important role in T3SS signaling.","tracks":[]}