| http://purl.uniprot.org/citations/18037438 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18037438 | http://www.w3.org/2000/01/rdf-schema#comment | "Phage T4 protects its DNA from the two-gene-encoded gmrS/gmrD (glucose-modified hydroxymethylcytosine restriction endonuclease) CT of pathogenic Escherichia coli, CT596, by injecting several hundred copies of the 76-amino-acid-residue nuclease inhibitor, IPI*, into the infected host. Here, the three-dimensional solution structure of mature IPI* is reported as determined by nuclear magnetic resonance techniques using 1290 experimental nuclear Overhauser effect and dipolar coupling constraints ( approximately 17 constraints per residue). Close examination of this oblate-shaped protein structure reveals a novel fold consisting of two small beta-sheets (beta1: B1 and B2; beta2: B3-B5) flanked at the N- and C-termini by alpha-helices (H1 and H2). Such a fold is very compact in shape and allows ejection of IPI* through the narrow 30-A portal and tail tube apertures of the virion without unfolding. Structural and dynamic measurements identify an exposed hydrophobic knob that is a putative gmrS/gmrD-binding site. A single gene from the uropathogenic E. coli UT189, which codes for a gmrS/gmrD-like UT fusion enzyme (with approximately 90% identity to the heterodimeric CT enzyme), has evolved IPI* inhibitor immunity. Analysis of the gmrS/gmrD restriction endonuclease enzyme family and its IPI* family phage antagonists reveals an evolutionary pathway that has elaborated a surprisingly diverse and specifically fitted set of coevolving attack and defense structures."xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2007.10.064"xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/author | "Black L.W."xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/author | "Weber D.J."xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/author | "Varney K.M."xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/author | "Wright N.T."xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/author | "Rifat D."xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/name | "J Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/pages | "720-734"xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/title | "Restriction endonuclease inhibitor IPI* of bacteriophage T4: a novel structure for a dedicated target."xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://purl.uniprot.org/core/volume | "375"xsd:string |
| http://purl.uniprot.org/citations/18037438 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18037438 |
| http://purl.uniprot.org/citations/18037438 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18037438 |
| http://purl.uniprot.org/uniprot/#_P03718-mappedCitation-18037438 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18037438 |
| http://purl.uniprot.org/uniprot/P03718 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/18037438 |