| http://purl.uniprot.org/citations/17699157 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17699157 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17699157 | http://www.w3.org/2000/01/rdf-schema#comment | "In pathogenic Gram-negative bacteria, many virulence factors are secreted via the two-partner secretion pathway, which consists of an exoprotein called TpsA and a cognate outer membrane translocator called TpsB. The HMW1 and HMW2 adhesins are major virulence factors in nontypeable Haemophilus influenzae and are prototype two-partner secretion pathway exoproteins. A key step in the delivery of HMW1 and HMW2 to the bacterial surface involves targeting to the HMW1B and HMW2B outer membrane translocators by an N-terminal region called the secretion domain. Here we present the crystal structure at 1.92 A of the HMW1 pro-piece (HMW1-PP), a region that contains the HMW1 secretion domain and is cleaved and released during HMW1 secretion. Structural analysis of HMW1-PP revealed a right-handed beta-helix fold containing 12 complete parallel coils and one large extra-helical domain. Comparison of HMW1-PP and the Bordetella pertussis FHA secretion domain (Fha30) reveals limited amino acid homology but shared structural features, suggesting that diverse TpsA proteins have a common structural domain required for targeting to cognate TpsB proteins. Further comparison of HMW1-PP and Fha30 structures may provide insights into the keen specificity of TpsA-TpsB interactions."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.M705750200"xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m705750200"xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Kim Y."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Kim Y."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Walkiewicz K."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Walkiewicz K."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Yokoyama T."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Yokoyama T."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Yeo H.J."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Yeo H.J."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Grass S."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Grass S."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Geme J.W."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/author | "Geme J.W."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/pages | "31076-31084"xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/pages | "31076-31084"xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/title | "The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion."xsd:string |
| http://purl.uniprot.org/citations/17699157 | http://purl.uniprot.org/core/title | "The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion."xsd:string |