| http://purl.uniprot.org/citations/36055198 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/36055198 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/36055198 | http://www.w3.org/2000/01/rdf-schema#comment | "Type 1 secretion systems (T1SSs) are widespread in pathogenic Gram-negative bacteria, extruding protein substrates following synthesis of the entire polypeptide. The Escherichia coli hemolysin A secretion system has long been considered a prototype in structural and mechanistic studies of T1SSs. Three membrane proteins-an inner membrane ABC transporter HlyB, an adaptor protein HlyD, and an outer membrane porin TolC-are required for secretion. However, the stoichiometry and structure of the complex are unknown. Here, cryo-electron microscopy (cryo-EM) structures determined in two conformations reveal that the inner membrane complex is a hetero-dodecameric assembly comprising three HlyB homodimers and six HlyD subunits. Functional studies indicate that oligomerization of HlyB and HlyD is essential for protein secretion and that polypeptides translocate through a canonical ABC transporter pathway in HlyB. Our data suggest that T1SSs entail three ABC transporters, one that functions as a protein channel and two that allosterically power the translocation process."xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2022.07.017"xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2022.07.017"xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/author | "Chen J."xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/author | "Chen J."xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/author | "Lee J."xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/author | "Lee J."xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/author | "Zhao H."xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/author | "Zhao H."xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/date | "2022"xsd:gYear |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/date | "2022"xsd:gYear |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/pages | "3329-3340.e13"xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/pages | "3329-3340.e13"xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/title | "The hemolysin A secretion system is a multi-engine pump containing three ABC transporters."xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/title | "The hemolysin A secretion system is a multi-engine pump containing three ABC transporters."xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/volume | "185"xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://purl.uniprot.org/core/volume | "185"xsd:string |
| http://purl.uniprot.org/citations/36055198 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/36055198 |
| http://purl.uniprot.org/citations/36055198 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/36055198 |
| http://purl.uniprot.org/citations/36055198 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/36055198 |
| http://purl.uniprot.org/citations/36055198 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/36055198 |