| http://purl.uniprot.org/citations/17051161 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17051161 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17051161 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/17051161 | http://www.w3.org/2000/01/rdf-schema#comment | "Escherichia coli GlpG is an integral membrane protein that belongs to the widespread rhomboid protease family. Rhomboid proteases, like site-2 protease (S2P) and gamma-secretase, are unique in that they cleave the transmembrane domain of other membrane proteins. Here we describe the 2.1 A resolution crystal structure of the GlpG core domain. This structure contains six transmembrane segments. Residues previously shown to be involved in catalysis, including a Ser-His dyad, and several water molecules are found at the protein interior at a depth below the membrane surface. This putative active site is accessible by substrate through a large 'V-shaped' opening that faces laterally towards the lipid, but is blocked by a half-submerged loop structure. These observations indicate that, in intramembrane proteolysis, the scission of peptide bonds takes place within the hydrophobic environment of the membrane bilayer. The crystal structure also suggests a gating mechanism for GlpG that controls substrate access to its hydrophilic active site."xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature05255"xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature05255"xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/author | "Zhang Y."xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/author | "Zhang Y."xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/author | "Ha Y."xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/author | "Ha Y."xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/pages | "179-180"xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/pages | "179-180"xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/title | "Crystal structure of a rhomboid family intramembrane protease."xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/title | "Crystal structure of a rhomboid family intramembrane protease."xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/volume | "444"xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://purl.uniprot.org/core/volume | "444"xsd:string |
| http://purl.uniprot.org/citations/17051161 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17051161 |
| http://purl.uniprot.org/citations/17051161 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17051161 |
| http://purl.uniprot.org/citations/17051161 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17051161 |